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Information on EC 3.1.3.53 - [myosin-light-chain] phosphatase
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EC Tree
3.1.3.53 [myosin-light-chain] phosphataseIUBMB Comments
The enzyme is composed of three subunits. The holoenzyme dephosphorylates myosin light chains and EC 2.7.11.18, myosin-light-chain kinase, but not myosin; the catalytic subunit acts on all three substrates.
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Word Map
- 3.1.3.53
-
contractile
- artery
-
rock
- rhoa
-
rho-kinase
- actin
- endothelial
-
rho-associated
- agonist
- hypertension
- cytoskeleton
- aorta
-
vasoconstriction
- mlc20
-
tension
-
tone
-
fasudil
-
myosin-binding
-
agonist-induced
- actomyosin
-
isometric
- phenylephrine
- cgmp
- mesenteric
-
vasorelaxation
- gizzard
-
cgmp-dependent
- pkg
-
ca2+-sensitization
-
phasic
-
vsmcs
- calyculin
-
ca2+-independent
-
subunit-1
-
actin-myosin
-
thrombin-induced
-
denuded
-
thiophosphorylation
-
nonmuscle
- myofilament
-
endothelium-denuded
- carbachol
-
rho-mediated
- meromyosin
-
precontracted
-
myographs
- 8-br-cgmp
-
cgmp-mediated
- medicine
-
rhoa-dependent
-
alpha-toxin-permeabilized
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
mypt1, myosin phosphatase, mlcp, hek-293 cell, mlc phosphatase, myosin phosphatase target subunit 1, ppp1r12a, myosin phosphatase targeting subunit 1, smpp-1m, smooth muscle myosin phosphatase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
MBS
mLC phosphatase
MLCP
MLCPase
-
-
-
-
MLCPPase
-
-
-
-
MP
myosin light chain kinase phosphatase
-
-
-
-
myosin light chain phosphatase
myosin phosphatase
myosin phosphatase targeting subunit 1
myosin-targeting protein 1
MYPT1
MYPT1-pT853
-
myosin light-chain phosphatase-targeting subunit at Thr853
phosphatase, myosin
-
-
-
-
phosphatase, myosin light-chain kinase
-
-
-
-
PP-1G
-
-
-
-
PP-1M
-
-
-
-
PP-2A
-
-
-
-
PP1
PPP1R12A
protein phosphatase 2A
-
-
-
-
SMMP
-
-
-
-
smooth muscle myosin phosphatase
-
-
-
-
smooth muscle phosphatase I-IV
-
-
-
-
SMP-I
-
-
-
-
SMP-II
-
-
-
-
SMP-III
-
-
-
-
SMP-IV
-
-
-
-
SMPP
-
-
-
-
[myosin-light-chain] phosphatase
MLCP
-
-
-
-
MP
-
-
-
-
myosin light chain phosphatase
-
-
-
-
myosin phosphatase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[myosin light-chain] phosphate + H2O = [myosin light-chain] + phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
additional information
hydrolysis of phosphoric ester
-
-
-
-
additional information
-
cardiac derived MYPT2 and smooth muscle derived MYPT2 have similar properties
additional information
-
MYTP1 binds the catalytic subunit of type 1 phosphatase delta, binds many proteins like myosin II, ezrin, radixin, moesin, a-adducin, tau, MAP, elongation factor-1a, ZIP kinase, RhoA-GTP, key reaction is dephosphorylation of myosin II but also in cell migration, cell division
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SYSTEMATIC NAME
IUBMB Comments
[myosin-light-chain]-phosphate phosphohydrolase
The enzyme is composed of three subunits. The holoenzyme dephosphorylates myosin light chains and EC 2.7.11.18, myosin-light-chain kinase, but not myosin; the catalytic subunit acts on all three substrates.
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CAS REGISTRY NUMBER
COMMENTARY
108658-39-5
-
86417-96-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
P-MLC20 + H2O
MLC20 + phosphate
P-MLC20: phospho-peptide mimicking MLC20(3-26:P-Ser19)
-
-
?
phosphorylated phoshorylase B + H2O
phosphorylase B + phosphate
-
myosin-associated PP-1M
-
?
[myosin regulatory light chain] phosphate + H2O
[myosin regulatory light chain] + phosphate
-
from chicken gizzard
-
-
?
histone deacetylase 7 phosphate + H2O
histone deacetylase 7 + phosphate
-
HDAC7, dephosphorylation induces reimport into the nucleus
-
-
?
histone deacetylase 7 phosphate + H2O
histone deacetylase 7 + phosphate
-
HDAC7, dephosphorylation induces reimport into the nucleus
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
isozyme PP-1M is more active towards native myosin than isolated myosin P-light-chains or phosphorylase A
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
PP-2A: 30fold more effective in dephosphorylating myosin P-light-chains than native myosin, 10fold more active towards myosin P-light-chains than phosphorylase A
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
muscle
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
muscle
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
muscle
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
38 kDa catalytic subunit PP1c and holoenzyme are active, the 130 kDa subunit M130 activates PP1c activity, effect of truncation mutants of M130 on PP1c activity
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
from bovine stomach
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
the 130 kDa subunit and the 20 kDa subunit enhance activity of the catalytic subunit towards heavy meromyosin or the isolated P-light-chain from smooth muscle
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
role in the variable coupling between force and myosin light chain phosphorylation
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
the 130 kDa subunit and the 20 kDa subunit enhance activity of the catalytic subunit towards heavy meromyosin or the isolated P-light-chain from smooth muscle
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
from smooth muscle
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
20 kDa myosin light chain
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
important role in regulating myofibroblast contraction, Rho/Rho kinase-mediated inhibition of MLCPPase is necessary for lysophosphatidic acid-promoted myofibroblast contraction, in contrast to smooth muscle cells, in which MLCPPase activity only regulates the sensitivity of the contractile response to Ca2+
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
muscle
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
holoenzyme and isolated catalytic subunit are active
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
SMP-I, -II, -III and -IV are active
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
38 kDa catalytic subunit PP1c and holoenzyme are active, the 130 kDa subunit M130 activates PP1c activity, effect of truncation mutants of M130 on PP1c activity
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
myosin regulatory light chain RLC from chicken gizzard, specificity of MLCP toward various phosphorylation sites of RCL, N-terminal region of RLC plays an important role in substrate recognition
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
reaction is a prerequisite for the actin activation of the myosin Mg2+-ATPase
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
dephosphorylation of the myosin regulatory light chain of myosin, which is phosphorylated at various sites at its N-terminal region
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
myosin regulatory light chain RLC from chicken gizzard, specificity of MLCP toward various phosphorylation sites of RCL, N-terminal region of RLC plays an important role in substrate recognition
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
dephosphorylation of the myosin regulatory light chain of myosin, which is phosphorylated at various sites at its N-terminal region
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
isozyme PP-1M is more active towards native myosin than isolated myosin P-light-chains or phosphorylase A
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
isozyme PP-1G dephosphorylates myosin, myosin P-light-chain and phosphorylase A at comparable rates
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
PP-2A: 30fold more effective in dephosphorylating myosin P-light-chains than native myosin, 10fold more active towards myosin P-light-chains than phosphorylase A
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
plays a critical regulatory role in the Ca2+ sensitivity of myosin phosphorylation and smooth muscle contraction
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
muscle
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
chicken gizzard 20 kDa myosin light-chain phosphate
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
from turkey gizzard
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
key smooth muscle regulatory protein, MLCP is required for muscle relaxation
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
muscle
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
-
-
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
110 kDa/21 kDa complex accelerates dephosphorylation induced by the catalytic subunit PP1C by 1.6fold, the N-terminal sequence 1-309 of the 110 kDa subunit is sufficient to enhance the PP1C activity in muscle
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
20 kDa myosin light chain
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
110 kDa/21 kDa complex accelerates dephosphorylation induced by the catalytic subunit PP1C by 1.6fold, the N-terminal sequence 1-309 of the 110 kDa subunit is sufficient to enhance the PP1C activity in muscle
-
?
myosin regulatory light-chain phosphate + H2O
myosin regulatory light-chain + phosphate
-
nonmuscle
-
-
?
myosin regulatory light-chain phosphate + H2O
myosin regulatory light-chain + phosphate
-
nonmuscle
-
-
?
myosin regulatory light-chain phosphate + H2O
myosin regulatory light-chain + phosphate
-
nonmuscle
-
-
?
phosphorylated glycogen synthase + H2O
glycogen synthase + phosphate
-
the 130 kDa subunit and the 20 kDa subunit suppress activity of the catalytic subunit towards phosphorylase A and glycogen synthase
-
-
?
phosphorylated glycogen synthase + H2O
glycogen synthase + phosphate
-
the 130 kDa subunit and the 20 kDa subunit suppress activity of the catalytic subunit towards phosphorylase A and glycogen synthase
-
-
?
phosphorylated heavy meromyosin + H2O
heavy meromyosin + phosphate
-
the 130 kDa subunit and the 20 kDa subunit enhance activity of the catalytic subunit towards heavy meromyosin or the isolated P-light-chain from smooth muscle
-
-
?
phosphorylated heavy meromyosin + H2O
heavy meromyosin + phosphate
-
the 130 kDa subunit and the 20 kDa subunit enhance activity of the catalytic subunit towards heavy meromyosin or the isolated P-light-chain from smooth muscle
-
-
?
phosphorylated heavy meromyosin + H2O
heavy meromyosin + phosphate
-
a chymotryptic fragment of myosin, only SMP-III and SMP-IV are active, SMP-I and SMP-II not
-
-
?
phosphorylated heavy meromyosin + H2O
heavy meromyosin + phosphate
-
from turkey gizzard
-
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
isoenzyme PP-1M is more active towards native myosin than isolated myosin P-light-chains or phosphorylase A
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
isoenzyme PP-2A: low activity with native myosin
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
from bovine stomach, P-myosin assembly is essential for SMMP activity
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
from turkey gizzard
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
catalytic subunit is active, holoenzyme not
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
myosin heavy chain plays a role in the smooth muscle MLCP-myosin regulatory light chain interaction, specificity toward myosin phosphorylated at various sites of the myosin regulatory light chain RLC, role of the N-terminal region of RLC in the dephosphorylation of myosin
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
only SMP-III and SMP-IV are active, SMP-I and SMP-II not
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
dephosphorylates myosin in vivo, dephosphorylation of the myosin regulatory light chain, which is phosphorylated at various sites at its N-terminal region
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
from turkey gizzard
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
myosin heavy chain plays a role in the smooth muscle MLCP-myosin regulatory light chain interaction, specificity toward myosin phosphorylated at various sites of the myosin regulatory light chain RLC, role of the N-terminal region of RLC in the dephosphorylation of myosin
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
dephosphorylates myosin in vivo, dephosphorylation of the myosin regulatory light chain, which is phosphorylated at various sites at its N-terminal region
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
isoenzyme PP-1G dephosphorylates myosin, myosin P-light-chain and phosphorylase A at comparable rates
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
isoenzyme PP-1M is more active towards native myosin than PP-1G
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
isoenzyme PP-1M is more active towards native myosin than isolated myosin P-light-chains or phosphorylase A
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
isoenzyme PP-2A: low activity with native myosin
-
?
phosphorylated myosin-light chain kinase + H2O
myosin light-chain kinase + phosphate
-
holoenzyme and isolated catalytic subunit are active, phosphorylated at 2 sites, in absence of bound calmodulin rapid dephosphorylation at both sites, in presence of bound calmodulin dephosphorylation of only one site
-
?
phosphorylated myosin-light chain kinase + H2O
myosin light-chain kinase + phosphate
-
autophosphorylated myosin light chain kinase is a good substrate for the kinase- and myosin-associated protein phosphatase KAMPPase
-
-
?
phosphorylated myosin-light chain kinase + H2O
myosin light-chain kinase + phosphate
-
SMP-I modulates the activity of myosin-light chain kinase
-
?
phosphorylated phoshorylase A + H2O
phosphorylase A + phosphate
-
PP-2A: 30fold more effective in dephosphorylating myosin P-light-chains than native myosin, 10fold more active towards myosin P-light-chains than phosphorylase A
-
?
phosphorylated phoshorylase A + H2O
phosphorylase A + phosphate
-
isoenzyme PP-1M is more active towards native myosin than isolated myosin P-light-chains or phosphorylase A
-
?
phosphorylated phoshorylase A + H2O
phosphorylase A + phosphate
-
38 kDa catalytic subunit PP1c
-
?
phosphorylated phoshorylase A + H2O
phosphorylase A + phosphate
-
PP-2A: 30fold more effective in dephosphorylating myosin P-light-chains than native myosin, 10fold more active towards myosin P-light-chains than phosphorylase A
-
?
phosphorylated phoshorylase A + H2O
phosphorylase A + phosphate
-
isoenzyme PP-1M is more active towards native myosin than isolated myosin P-light-chains or phosphorylase A
-
?
phosphorylated phoshorylase A + H2O
phosphorylase A + phosphate
-
isoenzyme PP-1G dephosphorylates myosin, myosin P-light-chains and phosphorylase A at comparable rates
-
?
phosphorylated phosphorylase kinase + H2O
phosphorylase kinase + phosphate
-
the 130 kDa subunit and the 20 kDa subunit suppress activity of the catalytic subunit towards phosphorylase A and glycogen synthase
-
-
?
phosphorylated phosphorylase kinase + H2O
phosphorylase kinase + phosphate
-
the 130 kDa subunit and the 20 kDa subunit suppress activity of the catalytic subunit towards phosphorylase A and glycogen synthase
-
-
?
regulatory myosin light-chain phosphate + H2O
regulatory myosin light-chain + phosphate
-
-
-
-
?
regulatory myosin light-chain phosphate + H2O
regulatory myosin light-chain + phosphate
-
-
-
-
?
[myosin light-chain] phosphate + H2O
[myosin light-chain] + phosphate
-
-
-
-
?
[myosin light-chain] phosphate + H2O
[myosin light-chain] + phosphate
-
substrate is phosphorylated Physarum myosin II
-
-
?
[myosin light-chain] phosphate + H2O
[myosin light-chain] + phosphate
-
-
-
-
?
[myosin light-chain] phosphate + H2O
[myosin light-chain] + phosphate
-
substrate is regulatory light chain (LC20) of myosin II, MLCP-mediated dephosphorylation of LC20 at Ser19
-
-
?
additional information
?
-
-
both gene products of protein phosphatase 1, PP1, (catalytic subunit of the myosin phosphatase) ppp1cba and ppp1cbb interact with Mypt1 (regulatory subunit of the myosin phosphatase) and assemble an active myosin phosphatase complex
-
-
?
additional information
?
-
-
enzyme binds to vesicles of acidic phospholipids, i.e. phosphatidylserine, phosphatidylinositol and phosphatidic acid, but not to neutral phospholipids, phosphatidylserine binding decreases by increasing ionic strength and Mg2+ concentration, phospholipid binding is associated with the C-terminal part of the 130/133 kDa myosin-binding subunit and the 20 kDa regulatory subunit
-
-
?
additional information
?
-
-
130 kDa subunit MLCPa: elongated structure with 3 globular domains connected by flexible strands
-
-
?
additional information
?
-
-
interactions among the 38 kDa catalytic subunit PP1c, the 130 kDa and the 20 kDa non-catalytic subunits M130 and M20 or fragments of them, M130 has 2 binding sites for PP1c: one site in the N-terminal 38 residues and a weaker site in the ankyrin repeats region, activation of phosphatase and binding of PP1c and substrate are properties of the N-terminal one-third of M130
-
-
?
additional information
?
-
-
involved in force regulation in smooth muscle, the relative expression of splice-in/splice-out myosin-targeting subunit isoforms determines the magnitude of agonist-induced force enhancement/Ca2+ sensitization
-
-
?
additional information
?
-
-
130 kDa subunit MLCPa: elongated structure with 3 globular domains connected by flexible strands
-
-
?
additional information
?
-
role of the heart-specific small regulatory subunit hHS-M21 of MLCP
-
-
?
additional information
?
-
-
thrombin activates the Rho/Rho kinase pathway to inactivate myosin light chain phosphatase as part of a signaling network that controls myosin light chain phosphorylation and contraction in endothelial cells
-
-
?
additional information
?
-
-
myosin phosphatase subunits protein phosphatase 1beta (PP1beta) and myosin phosphatase targeting subunit (Mypt1) interact with transcription factor Nkx2.5 and inhibit its transcriptional activity
-
-
?
additional information
?
-
-
KAMPPase: kinase- and myosin-associated protein phosphatase, functional multienzyme complex composed of a myofibrillar form of smooth muscle myosin light chain phosphatase and myosin light chain kinase with or without calmodulin, regulation of the phosphatase activity
-
-
?
additional information
?
-
-
two forms of SMP-I, the intact form and the catalytic subunit, may act in an opposite manner to regulate smooth muscle contraction in vivo
-
-
?
additional information
?
-
-
together with myosin light chain kinase key regulatory enzyme of smooth muscle
-
-
?
additional information
?
-
-
involved in the regulation of smooth muscle contraction, regulation of the MLCP activity
-
-
?
additional information
?
-
-
pulmonary hypertension down-regulates pulmonary vascular MLCP expression, the maintenance of a high pulmonary vascular resistance may be secondary to abnormalities in tissue content and/or activity of MLCP
-
-
?
additional information
?
-
-
studies with fragments of the 110 kDa subunit on their ability to regulate relaxation and 20 kDa myosin light-chain dephosphorylation of rabbit permeabilized portal vein induced by the catalytic subunit PP1C
-
-
?
additional information
?
-
-
insulin stimulates the binding of MRIP (myosin phosphatase Rho-interacting protein) to MYPT1 in a dose- and time-dependent manner, as determined by immunoprecipitation
-
-
?
additional information
?
-
-
studies with fragments of the 110 kDa subunit on their ability to regulate relaxation and 20 kDa myosin light-chain dephosphorylation of rabbit permeabilized portal vein induced by the catalytic subunit PP1C
-
-
?
additional information
?
-
-
studies with fragments of the 110 kDa subunit on their ability to regulate relaxation and 20 kDa myosin light-chain dephosphorylation of rabbit permeabilized portal vein induced by the catalytic subunit PP1C
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phosphorylated myosin-light chain kinase + H2O
myosin light-chain kinase + phosphate
-
SMP-I modulates the activity of myosin-light chain kinase
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
role in the variable coupling between force and myosin light chain phosphorylation
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
important role in regulating myofibroblast contraction, Rho/Rho kinase-mediated inhibition of MLCPPase is necessary for lysophosphatidic acid-promoted myofibroblast contraction, in contrast to smooth muscle cells, in which MLCPPase activity only regulates the sensitivity of the contractile response to Ca2+
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
reaction is a prerequisite for the actin activation of the myosin Mg2+-ATPase
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
dephosphorylation of the myosin regulatory light chain of myosin, which is phosphorylated at various sites at its N-terminal region
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
dephosphorylation of the myosin regulatory light chain of myosin, which is phosphorylated at various sites at its N-terminal region
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
plays a critical regulatory role in the Ca2+ sensitivity of myosin phosphorylation and smooth muscle contraction
-
?
myosin light-chain phosphate + H2O
myosin light-chain + phosphate
-
key smooth muscle regulatory protein, MLCP is required for muscle relaxation
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
dephosphorylates myosin in vivo, dephosphorylation of the myosin regulatory light chain, which is phosphorylated at various sites at its N-terminal region
-
?
phosphorylated myosin + H2O
myosin + phosphate
-
dephosphorylates myosin in vivo, dephosphorylation of the myosin regulatory light chain, which is phosphorylated at various sites at its N-terminal region
-
?
[myosin light-chain] phosphate + H2O
[myosin light-chain] + phosphate
-
-
-
-
?
[myosin light-chain] phosphate + H2O
[myosin light-chain] + phosphate
-
substrate is regulatory light chain (LC20) of myosin II, MLCP-mediated dephosphorylation of LC20 at Ser19
-
-
?
additional information
?
-
-
both gene products of protein phosphatase 1, PP1, (catalytic subunit of the myosin phosphatase) ppp1cba and ppp1cbb interact with Mypt1 (regulatory subunit of the myosin phosphatase) and assemble an active myosin phosphatase complex
-
-
?
additional information
?
-
-
involved in force regulation in smooth muscle, the relative expression of splice-in/splice-out myosin-targeting subunit isoforms determines the magnitude of agonist-induced force enhancement/Ca2+ sensitization
-
-
?
additional information
?
-
-
thrombin activates the Rho/Rho kinase pathway to inactivate myosin light chain phosphatase as part of a signaling network that controls myosin light chain phosphorylation and contraction in endothelial cells
-
-
?
additional information
?
-
-
myosin phosphatase subunits protein phosphatase 1beta (PP1beta) and myosin phosphatase targeting subunit (Mypt1) interact with transcription factor Nkx2.5 and inhibit its transcriptional activity
-
-
?
additional information
?
-
-
two forms of SMP-I, the intact form and the catalytic subunit, may act in an opposite manner to regulate smooth muscle contraction in vivo
-
-
?
additional information
?
-
-
together with myosin light chain kinase key regulatory enzyme of smooth muscle
-
-
?
additional information
?
-
-
involved in the regulation of smooth muscle contraction, regulation of the MLCP activity
-
-
?
additional information
?
-
-
pulmonary hypertension down-regulates pulmonary vascular MLCP expression, the maintenance of a high pulmonary vascular resistance may be secondary to abnormalities in tissue content and/or activity of MLCP
-
-
?
additional information
?
-
-
insulin stimulates the binding of MRIP (myosin phosphatase Rho-interacting protein) to MYPT1 in a dose- and time-dependent manner, as determined by immunoprecipitation
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(S)-2-methyl-1-[(4-methyl-5-isoquinolinyl)sulfonyl]-hexahydro-1H-1,4-diazepine
-
H-1152, 0.0003 mM produces a strong inhibition of basal MYPT1-pT853 by nearly 75%, KCl produces an approximate 1.75-2fold increase in MYPT1-pT853 in the presence and absence of H-1152
14-3-3beta protein
-
70% inhibition in the presence of 0.5 mM 14-3-3beta, dissociates MLCP from myosin II
-
acidic phospholipid
-
interaction of enzyme with acidic phospholipids inhibits activity toward phosphorylated myosin
-
arachidonic acid
-
inhibits SMPP-1M, dissociates the catalytic subunit from the native holoenzyme, inhibits the regulatory action of the 110 kDa/21 kDa subunit complex on the catalytic subunit PP1C activity, the C-terminal half of the 110 kDa subunit is required for inhibition
flavone
-
inhibits U46619-induced regulatory myosin light-chain phosphorylation
glycerol
-
inhibits SMMP activity, dissociates P-myosin primarily into an extended conformation
MgATP2-
-
inhibits SMMP activity towards P-myosin, disassembles P-myosin mostly into a folded conformation
phosphatidic acid
-
most effective inhibitor among acidic phospholipids, followed by phosphatidylserine and phosphatidylinositol, phosphorylated myosin as substrate
phosphatidylinositol
-
phosphatidic acid is the most effective inhibitor among acidic phospholipids, followed by phosphatidylserine and phosphatidylinositol, phosphorylated myosin as substrate
phosphatidylserine
-
phosphatidic acid is the most effective inhibitor among acidic phospholipids, followed by phosphatidylserine and phosphatidylinositol, phosphorylated myosin as substrate
smoothelin-like 1 protein
-
originally called CHASM (calponin homology-associated smooth muscle), 55% inhibition at 0.0025 mM, 75% inhibition at up to 0.02 mM
-
Ca2+
-
partial inhibition of SMP-I, only with myosin light chain as substrate
CPI-17
-
specific inhibitor predominantly expressed in smooth muscles and neurons, phosphorylation of CPI-17 at Thr38 is necessary and sufficient to convert the protein into a potent inhibitor of myosin phosphatase
-
diphosphate
-
SMP-I, catalytic subunit is more sensitive than holoenzyme, most potent inhibitor among the phosphate analogs
Mg2+
-
partial inhibition of SMP-I, only with myosin light chain as substrate
okadaic acid
-
more potent inhibitor of type 2A phosphatase than of type 1 phosphatase
okadaic acid
-
at 1 nM almost complete inhibition of PP-2A; PP-1: 0.001 mM, 88% inhibition
phospho-CPI-17
-
MLCP inhibitor protein, phosphorylation at Thr-38 of CPI-17 results in inhibition of MLCP activity
-
phospho-CPI-17
-
MLCP inhibitor protein, phosphorylation at Thr-38 of CPI-17 results in inhibition of MLCP activity; Rho kinase and protein kinase C phosphorylate CPI-17 at Thr-38, CPI-17 phosphorylation plays a role in MLCP regulation
-
additional information
-
elevation of cAMP and maximal cAMP-dependent protein kinase activation cause a 50% reduction in myosin II regulatory light chain phosphorylation and a 35% drop in isometric tension
-
additional information
-
increases in the ionic strength inhibit SMMP activity
-
additional information
-
inhibitory effect of several truncation mutants of the 130 kDa subunit M130 on the activity of the catalytic subunit PP1c, IC50 values
-
additional information
-
MLCP inhibition may occur through RhoA/Rhokinase and/or protein kinase C with phosphorylation of myosin phosphatase targeting subunit-1 and protein kinase C-potentiated phosphatase inhibitor (CPI-17), respectively
-
additional information
-
phosphorylation on Thr695 and Thr850 (inhibitory sites) result in inhibition
-
additional information
-
phosphorylation of myosin phosphatase targeting subunit on Thr696 and Thr853 (inhibitory sites) results in inhibition
-
additional information
-
inhibition of MLC phosphatase by either the catalytic subunit of MLC phosphatase, CS1beta, or myosin PPase targeting subunit 1, MYPT1, siRNA-based depletion results in significant attenuation of purine nucleotide (ATP and adenosine)-induced EC barrier enhancement
-
additional information
-
inhibitory effect of several truncation mutants of the 130 kDa subunit M130 on the activity of the catalytic subunit PP1c, IC50 values
-
additional information
-
relaxation of submaximally contracted mouse arteries with urocortin results in a decrease in phosphorylation of myosin light chain S19 by 60% and of enzyme regulatory subunit T696 and T850 by 28 and 52%, resp. Effect of urocortin is blocked by Rp-8-CPT-cAMPS and mimicked by Sp-5,6-DCl-cBIMPS
-
additional information
-
phosphorylation at Thr-695 of the MLCP regulatory subunit MYPT1 inhibits MLCP activity
-
additional information
-
phosphorylation of the myosin-binding subunit of MLCP at Thr-641 inhibits MLCP activity
-
additional information
-
forskolin, the phosphoinositide 3-kinase inhibitor 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one, LY 294002, and the Rho kinase inhibitor (R)-(+)-trans-N-(4-pyridyl)-4-(1-aminoethyl)-cyclohexanecarboxamide, Y27632, inhibit KCl-induced contraction in organ culture
-
additional information
-
pulmonary hypertension down-regulates pulmonary vascular MLCP expression
-
additional information
-
MLCP holoenzyme is inhibited by binding of 14-3-3beta protein to MYPT1, 14-3-3beta protein diminishes the binding between MYPT1 and myosin II, and abolishes MYPT1 localization at stress fibers
-
additional information
-
two major ROK phosphorylation sites, Thr697 and Thr855, on MYPT1 elicit MLCP inhibition. Phosphorylation of both sites inhibits MLCP activity. MYPT1-T855 phosphorylation may also interfere with the binding of MYPT1 to myosin
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
p116Rip
-
RhoA-binding protein, activates enzyme activity of the holoenzyme due to binding to MYPT 1 targeting subunit. Activation is specific to myosin as substrate
-
sodium nitroprusside
-
nitrovasodilator, increases MLCP activity in intact carotid media, mechanism
U46619
-
thromboxane A2 analogue at 10-7 mol/L, increases phosphorylation of MYPT1 and regulatory myosin light-chain
additional information
-
the activity of the catalytic subunit of MLCP, CSbeta, towards myosin depends on its associated regulatory subunit, namely myosin PPase targeting subunit 1, MYPT1
-
additional information
-
telokin facilitates the dissociation of the phosphatase or its catalytic subunit from myosin light chain kinase oligomers increasing the MLCPase activity of the multienzyme complex, but no effect on the activity of the purified MLCPase holoenzyme or its catalytic subunit
-
additional information
-
C-terminal leucine-zipper of MYPT 1 subunit is required for cGMP-mediated activation of enzyme
-
additional information
-
rhoA kinase 1 and rhoA kinase 2 isoforms both regulate MLCP phosphorylation
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01
[myosin light-chain] phosphate
-
pH 7.6, temperature not specified in the publication
0.00103
myosin light-chain phosphate
-
smooth muscle, type 1 protein phosphatase delta and MYPT1
0.00136
myosin light-chain phosphate
-
smooth muscle, type 1 protein phosphatase delta and MYPT2
0.00394
myosin light-chain phosphate
-
smooth muscle, type 1 protein phosphatase delta only
0.00502
myosin light-chain phosphate
-
cardiac muscle, type 1 protein phosphatase delta and MYPT1
0.00551
myosin light-chain phosphate
-
cardiac muscle, type 1 protein phosphatase delta and MYPT2
0.01117
myosin light-chain phosphate
-
cardiac muscle, type 1 protein phosphatase delta only
0.0024
Phosphorylated myosin
-
at a ionic strength of 0.15 M, in the presence of 0.1 mM MgATP
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000011
phosphorylated fragment 654-880 of human myosin phosphatase targeting subunit GST-fusion
Sus scrofa
-
-
-
0.00006
phosphorylated fragment 697-880 of human myosin phosphatase targeting subunit GST-fusion
Sus scrofa
-
-
-
0.0014
unphosphorylated fragment 654-880 of human myosin phosphatase targeting subunit GST-fusion
Sus scrofa
-
-
-
0.0061
unphosphorylated fragment 697-880 of human myosin phosphatase targeting subunit GST-fusion
Sus scrofa
-
-
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.028
-
purified enzyme, pH 7.6, temperature not specified in the publication
additional information
additional information
dephosphorylation activity of myosin phosphatase immunoprecipitated from the apoptotic cells is lower than that from nonapoptotic control cells
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
7
-
dephosphorylation of intact myosin or isolated myosin light-chain by the catalytic subunit
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
25
-
assay at, dephosphorylation of myosin light chain kinase in presence or absence of calmodulin bound to the kinase
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
normal and pulmonary hypertensive fetal sheep, MLCP, protein phosphatase type 1
-
-
brenda
mutant in the myosin phosphatase-targeting subunit Mbs enhances the lethality of flapwing, flw, and JNK phosphatase puckered, puc, mutants
-
-
brenda
wild type, DMBS null mutants and transheterozygotes with stronger and weaker alleles
-
-
brenda
-
-
-
brenda
heart-specific small regulatory subunit isoform hHS-M21 A of MLCP
SwissProt
brenda
heart-specific small regulatory subunit isoform hHS-M21 B of MLCP
SwissProt
brenda
4 different protein phosphatases are active towards isolated myosin light-chains: SMP-I, SMP-II, SMP-III, SMP-IV
-
-
brenda
KAMPPase: kinase- and myosin-associated protein phosphatase, a myofibrillar form of smooth muscle myosin light chain phosphatase forms a multienzyme complex with myosin light chain kinase
-
-
brenda
myosin-bound form PP-1M, glycogen-bound form PP-1G and PP-2A
-
-
brenda
Sprague-Dawley, virgin rat, pregnant rat, in pregnant rats with hypertension
-
-
brenda
89.6 kDa fragment of MYPT1, an isoform of the 130 kDa regulatory subunit of myosin phosphatase
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
normal and pulmonary hypertensive fetal sheep, pulmonary artery, aorta and vena cava
brenda
-
lung pulmonary artery, enzyme specific activity is related to Rho-kinase activation during lung morphogenesis
brenda
-
from venous blood, myosin phosphatase in platelets is composed of the catalytic subunit of PP-1 plus a subunit similar to the 130 kDa regulatory myosin-binding subunit of the smooth muscle phosphatase, major phosphatase is PP-1, also PP-2A
brenda
-
fetal, MLCP activity in pulmonary hypertensive fetal sheep is significantly lower than in normal fetal sheep
brenda
-
rat embryonic fibroblast cells, mitotic, 133 kDa myosin-binding subunit
brenda
-
mesenteric vein, high expression of enzyme with predominance of 3-exon-excluded, leucine-zipper negative MYPT 1 isoform
brenda
-
fetal, same MLCP activities in normal and pulmonary hypertensive fetal sheep
brenda
additional information
expression profiles of the heart-specific small subunit hHS-M21 and of the large myosin-binding subunit of MLCP
brenda
-
embryonic and adult, smooth muscle, throughout development, exclusive expression of the splice-in myosin-targeting subunit isoform
brenda
-
fetal, same MLCP activities in normal and pulmonary hypertensive fetal sheep
brenda
-
and large capacitance vessels, predominantly expression of 3-exon-out/leucine-zipper positive MYPT 1 isoform
brenda
-
expression of leucine-zipper positive isoform of MYPT 1 predominantes in healthy animal
brenda
-
first-order mesenteric resistance artery, high expression of enzyme with predominance of 3-exon-excluded, leucine-zipper negative MYPT 1 isoform
brenda
-
iliac artery, expression of leucine-zipper positive isoform of MYPT 1 predominates in healthy animal
brenda
-
intrapulmonary arterial tissue, enzyme protein increases with age and is highest in adult rat. In contrast, enzyme specific activity is significantly higher in fetal compared with adult tissue
brenda
-
pulmonary artery, predominantly expression of 3-exon-out/leucine-zipper positive MYPT 1 isoform
brenda
-
expression of MYPT1 and MYPT2, the 2 isoforms of the large subunit
brenda
-
isoenzyme PP-1M accounts for 90% of the myosin phosphatase activity, isoenzyme PP-1G is essentially absent
brenda
the small regulatory subunit hHS-M21 is expressed only in cardiac muscle, not in smooth muscle
brenda
-
embryonic and adult, early during development, expression of the splice-in myosin-targeting subunit isoform, then shift from the splice-in to the splice-out isoform, exclusive expression of the splice-out isoform in adult chicken
brenda
-
expression of MYPT1 and MYPT2, the 2 isoforms of the large subunit
brenda
-
portal vein, expression of MYPT 1 subunit increases 2fold between postnatal days 6 and 12 with similar increase in enzyme activity. MYPT 1 switches from leucine-zipper positive to leucine-zipper negative isoforms, concordant with a switch from sensitive to resisitant to cGMP-mediated vascular relaxation
brenda
-
granuloma pouch model of granulation tissue, organ culture
brenda
-
granuloma pouch model of granulation tissue, organ culture
-
brenda
-
phasic portal vein and vas deferens smooth muscles
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
subunit MYPT1, in confluent endothelial cells, at the cell membrane and cell-cell contacts
-
brenda
-
depending on fixation method for immunohistochemistry, localization of myosin phosphatase target subunit found in nucleus, nucleolus, or cytoplasm
brenda
-
enzyme may interact with membranes, phosphorylation by protein kinase A may modify interaction, distribution of the 130/133 kDa myosin-binding subunit at the membrane
brenda
-
depending on fixation method for immunohistochemistry, localization of myosin phosphatase target subunit found in nucleus, nucleolus, or cytoplasm
brenda
additional information
-
PP-1M activity is associated with the myofibrillar fraction
brenda
-
myofibrillar form of smooth muscle myosin light chain phosphatase forms a multienzyme complex with myosin light chain kinase
brenda
-
PP-1M activity is associated with the myofibrillar fraction
brenda
-
full-length enzyme and deletion mutants that contain the N-terminal nuclear localization signal
brenda
-
depending on fixation method for immunohistochemistry, localization of myosin phosphatase target subunit found in nucleus, nucleolus, or cytoplasm
brenda
additional information
-
subcellular localization of the large subunit MYPT in embryo fibroblasts
-
brenda
additional information
-
localization of PP-1 and PP-2A and their subunits in platelets
-
brenda
additional information
subcellular localization of the subunit MYPT1 in growing and confluent endothelial cells
-
brenda
additional information
-
subcellular localization of the subunit MYPT1 in growing and confluent endothelial cells
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
-
phosphorylation of MYPT1 is a major mechanism of MLCP regulation, but protein-protein interactions may also be important. Ca2+-dependent and Rho-associated kinase-mediated regulation of myosin light chain kinase and myosin light chain phosphatase, respectively, in the arterial myogenic response, molecular mechanisms, overview
physiological function
additional information
malfunction
-
a loss-of-function mutation of flapwing, which encodes the catalytic subunit of protein phosphatase 1beta, disrupts oocyte polarization. Proliferation and differentiation of the posterior follicle cells are affected by FP41, also FP41 mutation disrupts cell differentiation and Notch signaling of the cells. Excessive myosin activity in the posterior follicle cells causes oocyte mispolarization and defective Notch signaling and endocytosis in the posterior follicle cells, phenotype, detailed overview. The Notch intracellular domain can rescue the Notch signaling phenotype, but not the oocyte polarity phenotype of flwFP41 mutant cells
malfunction
deletion of MYPT1 in vascular smooth muscle enhances RLC (myosin regulatory light chain) phosphorylation and contractile activity, which may contribute to the development of hypertension in vivo
malfunction
knockdown of MYPT1 does not cause apoptosis in normal HeLa cells but the percentage of TNF/CHX-induced apoptotic cells is increased in MYPT1-depleted cells
malfunction
-
Morpholino knock-down of ppp1cba and ppp1cbb results in severe defects in morphogenetic cell movements during gastrulation through loss of myosin phosphatase function
physiological function
-
MLCP is directly and critically involved in endothelial cell barrier regulation, enhancement, and protection, with involvement of catalytic enzyme subunit CS1beta in the endothelial cell barrier enhancement induced by extracellular purines
physiological function
-
myosin phosphatase is required for contractile ring disassembly at the end of cytokinesis, it is involved in the assembly of ring canals derived from incomplete cytokinesis and function as intracellular bridges between nurse cells, thereby allowing cytoplasmic flow from nurse cells to oocytes. Myosin phosphatase must be temporally controlled during cytokinesis: it is first inactivated for the activation of a contractile ring at the initial stage of cytokinesis and then inactivated for the disassembly of the contractile ring
physiological function
-
physiological roles of myosin light chain kinase, MLCK, activation and myosin light chain phosphatase, MLCP, inhibition in the myogenic response, MLCP inhibition may also be required to slow the rate of LC20 dephosphorylation, mechanism, overview
physiological function
-
PP1beta, by regulating myosin activity, controls the generation of the oocyte polarizing signal, it is essential for dephosphorylation and inactivation of the non-muscle myosin II light chain encoded by spaghetti squash. PP1beta regulates the membrane levels of apical complexes in the posterior follicle cells
physiological function
-
the heart-specific small subunit, hHS-M21, is a heart-specific effector of Rho-associated kinase and plays a regulatory role in the MYPT1 phosphorylation at Thr-696 by Rho-associated kinase, molecular mechanism, overview
physiological function
-
Par-1 (cell polarity protein) binds to myosin phosphatase and phosphorylates it at a known inactivating site. Par-1 thus promotes phosphorylated myosin regulatory light chain, thereby increasing Myo-II activity
physiological function
as motor axons exit from the spinal cord and extend through extracellular matrix produced by adjacent notochord cells,these cells shift several cell diameters caudally. Individual motoneuron cell bodies stay aligned with their extending axons. This alignment requires myosin phosphatase activity within motoneurons, and mutations in the myosin phosphatase subunit Mypt1 increase myosin phosphorylation causing a displacement between motoneuron cell bodies and their axons
physiological function
-
differences in MYPT1 exon 24 isoforms, endothelial nitric oxide synthase eNOS, and potassium ion channel Kir2.1 distinguish epicardial arteries and resistance coronary arterioles. MYPT1 isoforms are distinct in the epicardial arteries (exon 24 -/leucine zipper +) and resistance arterioles (exon 24 +/leucine zipper -) and unchanged by exercise training or coronary occlusion. MYPT1, CPI-17 and PDE5 mRNA levels are not different between arteries and arterioles while Kir2.1 and eNOS are 6.6fold and 3.9fold higher in the arterioles
physiological function
interaction of myosin phosphatase target subunit (MYPT1) and myosin phosphatase-RhoA interacting protein (MRIP) causes colocalization of myosin phosphatase and RhoA to actomyosin. The residues 724-837 of MRIP are sufficient for the MYPT1/MRIP interaction. MRIP binds to MYPT1 as either a monomer or a dimer. The leucine repeat region of MYPT1, LR (residues 991-1030) is sufficient to account for the MYPT1/MRIP interaction. Point mutations that replace glutamic acids 998-1000 within LR reduce the binding affinity toward MRIP
physiological function
-
myosin light-chain phosphatase subunit flapwing (flw) is a key regulator of basal myosin oscillations and cell contractions underlying egg chamber elongation. Flw expression decreases specifically on the basal side of follicle cells at the onset of contraction and flw controls the initiation and periodicity of basal actomyosin oscillations
physiological function
phosphorylation of MYPT1 residue T694, but not T852, is a primary mechanism contributing to inhibition of myosin light chain phosphatase activity and enhancement of myosin regulatory light chain phosphorylation in vivo. Smooth muscles containing the T694A mutation show a significant reduction of force along with reduced myosin regulatory light chain phosphorylation. The contractile responses of the T694A mutant smooth muscle are independent of RhoA-associated protein kinase ROCK activation
physiological function
Rho family G-proteinRac1 inhibits the activity of myosin light chain phosphatase MLCP through a phosphatase that targets MYPT1 and specific inhibitor CPI-17 rather than through the RhoA-Rho dependent kinase (ROCK) pathway. Rac1 inhibition decreases agonist-induced increase in myosin light chain phosphorylation
physiological function
silencing of, the regulatory subunit of myosin phosphatase MYPT1 has a negative impact on the migration of keratinocytes during wound closure and it influences the cell-cell adhesion properties by decreasing the impedance of HaCaT cells. Myosin phosphatase contributes to the mediation of wound healing by regulating the Akt signaling pathway
physiological function
silencing of, the regulatory subunit of myosin phosphatase MYPT1 has a negative impact on the migration of keratinocytes during wound closure and it influences the cell-cell adhesion properties by decreasing the impedance of HaCaT cells. Myosin phosphatase contributes to the mediation of wound healing by regulating the Akt signaling pathway
physiological function
-
transgenic mice with cardiac-specific overexpression of heart-specific small subunit of myosin light chain phosphatase hHS-M21 show increased Ca2+ sensitivity of cardiac muscle contraction in vivo, which is not followed by an increased phosphorylation of myosin light chain 2 isoforms. hHS-M21 transgenic mice developed severe systolic dysfunction with myocardial fibrosis and degeneration of cardiomyocytes in association with sinus bradycardia and atrioventricular conduction defect. The contractile dysfunction and cardiac fibrosis are improved by treatment with the Rho kinase inhibitor fasudil
physiological function
-
treatment of Triton-skinned rat caudal arterial smooth muscle strips with the membrane-impermeant phosphatase inhibitor microcystin or treatment of intact tissue with the membrane-permeant phosphatase inhibitor calyculin A induces slow, sustained contractions that correlate with phosphorylation of MYPT1 at 7 to more than 10 sites
physiological function
variants of myosin light chain phosphatase regulatory subunit Mypt1 are generated by alternative splicing of the 31 nt exon 24, i.e. E24. In mice that underwent Tamoxifen-inducible and smooth muscle-specific knockout of E24 after weaning, deletion of a single allele of E24 enhances vasorelaxation of first-order mesenteric arteries to diethylamine-NONOate and to cGMP in permeabilized and calcium-clamped arteries and lowers blood pressure. First-order mesenteric arteries from homozygous E24 knockout mice show reduced force generation to alpha-adrenergic activation. 2 weeks of high-salt diet increase mesenteric arteries force generation to phenylephrine in control mice, which is markedly suppressed in the E24 knockout homozygotes
additional information
-
myosin II association with actin, which triggers contraction, is regulated by orchestrated waves of phosphorylation/dephosphorylation of the myosin regulatory light chain. Dephosphorylation is mediated by myosin phosphatase
additional information
-
myosin light chain phosphatase is regulated by phosphorylation of the catalytic subunit, the heart-specific small subunit, hHS-M21, plays a role in the regulation by phosphorylation, molecular mechanism, overview. Two isoforms of hHSM21, hHS-M21Aand hHS-M21B, preferentially bound the C-terminal one-third region of MYPT1 and MYPT2, respectively. Amino acid substitutions at a phosphorylation site of MYPT1, Ser852, impaired the binding of MYPT1 and hHS-M21. The hHS-M21 increases the phosphorylation level of MYPT1 at Thr696, which is attenuated by Rho-associated kinase, ROCK, inhibitors and small interfering RNAs for Rho-associated kinase
additional information
-
regulation of the enzyme involving ERM proteins ezrin, radixin, moesin, and isozymes of myosin PPase targeting subunit 1, MYPT1, overview
additional information
-
smooth muscle myosin light chain phosphatase, MLCP, consists of three proteins, the catalytic PP1c-delta phosphatase, the MYPT1 targeting subunit, and M20 protein. Binding of PP1c-delta to MYPT1 occurs via a RVXF motif immediately adjacent to a series of ankyrin repeats that are implicated in protein-protein interactions. Myosin binding may occur over a region at the C-terminus that contains one of the two major ROK phosphorylation sites, T697 and T855. MYPT1 is a substrate for phosphorylation by several serine/threonine kinases that modulate MLCP activity and/or alter myosin binding. MYPT1 has three essential functions: (i) to confer myosin substrate specificity to the complex, (ii) to enhance the specific activity of PP1c-delta in dephosphorylating phospho-LC20, and (iii) to provide a means by which MLCP activity can be regulated by a variety of stimuli
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PP1B_BOVIN
327
0
37187
Swiss-Prot
other Location (Reliability: 2)
PP1B_CANLF
327
0
37187
Swiss-Prot
other Location (Reliability: 2)
PP1B_CHICK
327
0
37187
Swiss-Prot
other Location (Reliability: 2)
PP1B_HUMAN
327
0
37187
Swiss-Prot
other Location (Reliability: 2)
PP1B_MOUSE
327
0
37187
Swiss-Prot
other Location (Reliability: 2)
PP1B_PIG
327
0
37187
Swiss-Prot
other Location (Reliability: 2)
PP1B_PONAB
327
0
37187
Swiss-Prot
other Location (Reliability: 2)
PP1B_RABIT
327
0
37187
Swiss-Prot
other Location (Reliability: 2)
PP1B_RAT
327
0
37187
Swiss-Prot
other Location (Reliability: 2)
Q4EAN6_9RICK
152
0
16784
TrEMBL
-
A0A803KK91_XENTR
186
0
21234
TrEMBL
Mitochondrion (Reliability: 5)
B3GXM3_ACTP7
Actinobacillus pleuropneumoniae serotype 7 (strain AP76)
547
0
60896
TrEMBL
-
MYPT2_HUMAN
982
0
110404
Swiss-Prot
other Location (Reliability: 2)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
130000
150000
-
kinase- and myosin-associated protein phosphatase KAMPPase, gel filtration
20000
21000
-
1 * 110000 + 1 * 37000 + 1 * 21000, enzyme SMPP-1M, 37 kDa catalytic subunit PP1C, 110 kDa regulatory subunit M110
230000
37000
38000
55000
-
x * 60000 + x * 55000 + x * 38000, 38 kDa catalytic subunit, ratio 1:1:1, enzyme SMP-I, SDS-PAGE
60000
-
x * 60000 + x * 55000 + x * 38000, 38 kDa catalytic subunit, ratio 1:1:1, enzyme SMP-I, SDS-PAGE
67000
-
x * 37000 + x * 67000, 37 kDa catalytic subunit, 67 kDa targeting subunit binds to the catalytic subunit, to myosin light chain kinase and Ca2+-independently to calmodulin, ratio of subunits 1:2, MLCPase of the multienzyme complex with myosin light chain kinase is named KAMPPase, SDS-PAGE
110000
-
1 * 110000 + 1 * 37000 + 1 * 21000, enzyme SMPP-1M, 37 kDa catalytic subunit PP1C, 110 kDa regulatory subunit M110
130000
-
1 * 130000 + 1 * 38000 + 1 * 20000, 38 kDa catalytic subunit is the type 1delta isoform, 130 kDa regulatory subunit binds myosin and the catalytic subunit, amino acid sequences
130000
-
x * 130000 + x * 37000 + x * 20000, 37 kDa catalytic subunit, ratio 1:1:1, SDS-PAGE
130000
-
x * 130000 + x * 38000 + x * 20000, 38 kDa catalytic subunit PP1c, 130 kDa and 20 kDa non-catalytic subunits M130 and M20, investigation of the interactions among PP1c, M20 and various mutants of M130 using the yeast two-hybrid system
130000
-
x * 130000 + x * 38000 + x * 20000, 130 kDa regulatory myosin-binding subunit, 38 kDa catalytic subunit, 20 kDa regulatory subunit, SDS-PAGE
20000
-
1 * 130000 + 1 * 38000 + 1 * 20000, 38 kDa catalytic subunit is the type 1delta isoform, 130 kDa regulatory subunit binds myosin and the catalytic subunit, amino acid sequences
20000
-
x * 130000 + x * 37000 + x * 20000, 37 kDa catalytic subunit, ratio 1:1:1, SDS-PAGE
20000
-
x * 130000 + x * 38000 + x * 20000, 38 kDa catalytic subunit PP1c, 130 kDa and 20 kDa non-catalytic subunits M130 and M20, investigation of the interactions among PP1c, M20 and various mutants of M130 using the yeast two-hybrid system
20000
-
x * 130000 + x * 38000 + x * 20000, 130 kDa regulatory myosin-binding subunit, 38 kDa catalytic subunit, 20 kDa regulatory subunit, SDS-PAGE
37000
-
1 * 110000 + 1 * 37000 + 1 * 21000, enzyme SMPP-1M, 37 kDa catalytic subunit PP1C, 110 kDa regulatory subunit M110
37000
-
x * 130000 + x * 37000 + x * 20000, 37 kDa catalytic subunit, ratio 1:1:1, SDS-PAGE
37000
-
x * 37000 + x * 67000, 37 kDa catalytic subunit, 67 kDa targeting subunit binds to the catalytic subunit, to myosin light chain kinase and Ca2+-independently to calmodulin, ratio of subunits 1:2, MLCPase of the multienzyme complex with myosin light chain kinase is named KAMPPase, SDS-PAGE
38000
-
1 * 130000 + 1 * 38000 + 1 * 20000, 38 kDa catalytic subunit is the type 1delta isoform, 130 kDa regulatory subunit binds myosin and the catalytic subunit, amino acid sequences
38000
-
x * 60000 + x * 55000 + x * 38000, 38 kDa catalytic subunit, ratio 1:1:1, enzyme SMP-I, SDS-PAGE
38000
-
x * 130000 + x * 38000 + x * 20000, 38 kDa catalytic subunit PP1c, 130 kDa and 20 kDa non-catalytic subunits M130 and M20, investigation of the interactions among PP1c, M20 and various mutants of M130 using the yeast two-hybrid system
38000
-
x * 130000 + x * 38000 + x * 20000, 130 kDa regulatory myosin-binding subunit, 38 kDa catalytic subunit, 20 kDa regulatory subunit, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotrimer
trimer
additional information
?
-
x * 130000 + x * 38000 + x * 20000, 38 kDa catalytic subunit PP1c, 130 kDa and 20 kDa non-catalytic subunits M130 and M20, investigation of the interactions among PP1c, M20 and various mutants of M130 using the yeast two-hybrid system
?
-
x * 130000 + x * 38000 + x * 20000, 130 kDa regulatory myosin-binding subunit, 38 kDa catalytic subunit, 20 kDa regulatory subunit, SDS-PAGE
?
-
x * 130000 + x * 38000 + x * 20000, 130 kDa regulatory myosin-binding subunit, 38 kDa catalytic subunit, 20 kDa regulatory subunit, SDS-PAGE
-
?
-
x * 60000 + x * 55000 + x * 38000, 38 kDa catalytic subunit, ratio 1:1:1, enzyme SMP-I, SDS-PAGE
?
-
x * 37000 + x * 67000, 37 kDa catalytic subunit, 67 kDa targeting subunit binds to the catalytic subunit, to myosin light chain kinase and Ca2+-independently to calmodulin, ratio of subunits 1:2, MLCPase of the multienzyme complex with myosin light chain kinase is named KAMPPase, SDS-PAGE
heterotrimer
-
1 * 130000 + 1 * 38000 + 1 * 20000, 38 kDa catalytic subunit is the type 1delta isoform, 130 kDa regulatory subunit binds myosin and the catalytic subunit, amino acid sequences
heterotrimer
-
x * 130000 + x * 37000 + x * 20000, 37 kDa catalytic subunit, ratio 1:1:1, SDS-PAGE
heterotrimer
-
gizzard MP, 3 subunits: the two isoforms of the large subunit M130/M133 differ by a central insert at residues 512-552, the catalytic subunit PP1c delta isoform, two isoforms of the small subunit M20/M21 differing in the C-terminal sequence and in the presence or absence of leucin zipper motifs
heterotrimer
-
x * 130000 + x * 37000 + x * 20000, 37 kDa catalytic subunit, ratio 1:1:1, SDS-PAGE
-
heterotrimer
-
1 * 110000 + 1 * 37000 + 1 * 21000, enzyme SMPP-1M, 37 kDa catalytic subunit PP1C, 110 kDa regulatory subunit M110
heterotrimer
-
1 * 110000 + 1 * 37000 + 1 * 21000, enzyme SMPP-1M, 37 kDa catalytic subunit PP1C, 110 kDa regulatory subunit M110
-
trimer
-
myosin light chain phosphatase consists of a catalytic subunit, a large subunit, MYPT1 or MYPT2, and a small subunit
trimer
-
smooth muscle MLCP is a trimeric holoenzyme complex composed of 38 kDa PP1c-delat phosphatase, 110-130 kDa regulatory, myosin-targeting subunit, MYPT1, and a small, 20 kDa M20 subunit, presence of an acid residue cluster and LZ the presence of leucine zipper motifs in the LZ+ MYPT1 splice variant
additional information
-
MLCP is a heterotrimer composed of the catalytic subunit belonging to protein phosphatase 1c PPC1, the myosin-binding subunit MBS, and M20
additional information
-
the myosin-targeting subunit MYPT has 2 isoforms produced by alternative splicing that differ by a central insert: 133 kDa splice-in and 130 kDa splice-out isoform, expression of the MYPT isoforms is both developmentally regulated and tissue-specific
additional information
-
structure and molecular properties of the 18.5 kDa isoform of the small subunit of MP with 21 kDa on SDS-PAGE and 18.4 kDa predicted from the amino acid sequence, 2 isoforms: 18.5 and 21 kDa, the small and the 107 kDa targeting subunit form a complex as 1:1 heterodimer
additional information
-
structure and molecular properties of the 18.5 kDa isoform of the small subunit of MP with 21 kDa on SDS-PAGE and 18.4 kDa predicted from the amino acid sequence, 2 isoforms: 18.5 and 21 kDa, the small and the 107 kDa targeting subunit form a complex as 1:1 heterodimer
-
additional information
the heart-specific small regulatory subunit hHS-M21 of MLCP increases the Ca2+ sensitivity in muscle and binds to the large myosin-binding subunit, it plays a regulatory role in cardiac muscle contraction by its binding to the large subunit MBS, MBS encoded by the MYPT1 gene, not by MYPT2, is the main target subunit of hHS-M21
additional information
-
The leucine-zipper motif at the N terminus of PKG forms a homodimeric coiled coil, the one at the C terminus of MYPT1 is monomeric and non-helical. The leucine-zipper motif of PKG binds to that of MYPT1 to form a heterodimer. When the leucine-zipper motif of MYPT1 is absent, the PKG leucine-zipper motif binds to the coiled coil region and upstream segments of MYPT1 via formation of a heterotetramer
additional information
-
myosin phosphatase is a complex that consists of a catalytic subunit protein phosphatase 1c, PP1cbeta, a large subunit myosin phosphatase targeting subunit, MYPT, and a small subunit. Stability of PP1cbeta and MYPT1 is interdependent, knocking down one of the subunits decreases the expression level of the other. MYPT1 binding is restricted to PP1cbeta, the central region of PP1cbeta confers the isoform-specific binding, while the variable, C-terminal domain of PP1cbeta is the region key for isoform-specific interaction with MYPT1. Sequence comparison of PP1 isoforms, overview
additional information
-
enzyme has 3 subunits, the catalytic subunit type 1 protein phosphatase delta, the regulatory subunit MYPT1 and a small subunit M20
additional information
-
enzyme has 3 subunits, the catalytic subunit type 1 protein phosphatase delta, the regulatory subunit MYPT1 in smooth muscle and MYPT 2 an isoform of MYPT1 in striated muscle
additional information
-
myosin phosphatase is a heterotrimer composed of the catalytic subunit belonging to protein phosphatase 1 PP1, the myosin phosphatase targeting subunit MYPT1, and M21
additional information
-
myosin phosphatase is a heterotrimer composed of the catalytic subunit belonging to protein phosphatase 1 PP1, the myosin phosphatase targeting subunit MYPT1, and M21
-
additional information
-
MLCP is a heterotrimer composed of the catalytic subunit belonging to protein phosphatase 1c PPC1, the myosin phosphatase targeting subunit MYPT1, and M21
additional information
-
myosin phosphatase is a heterotrimer composed of the catalytic subunit belonging to protein phosphatase 1 PP1, the myosin phosphatase targeting subunit MYPT1, and M21
additional information
-
MLCP is a heterotrimer composed of the catalytic subunit belonging to protein phosphatase 1c PPC1, the myosin phosphatase targeting subunit MYPT1, and M21
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
proteolytic modification
phosphoprotein
-
Par-1 (cell polarity protein) activates Myo-II by phosphorylating and inhibiting the myosin phosphatase complex
phosphoprotein
-
130/133 kDa myosin-binding subunits M130/M133 and 20 kDa regulatory subunit M20 are phosphorylated by protein kinase A to 3 and 1 mol phosphate/mol of subunit, phosphorylation of holoenzyme decreases phospholipid binding, M130/133: C-terminal phosphorylation site involved in regulation of phospholipid binding, no phosphorylation of the catalytic subunit PP-1cdelta, protein kinase C also phosphorylates M130/M133 and M20, but no effect on binding of phospholipids
phosphoprotein
-
inhibition of enzyme activity by phosphorylation of its myosin-targeting subunit, only in adult gizzard, not in adult aortic smooth muscle, phosphorylation is not required for Ca2+ sensitization of force
phosphoprotein
-
Thr-654 and Thr-695 are the major phosphorylation sites of the large subunit MYPT isoforms M130 and M133
phosphoprotein
phosphorylation of MYPT1 by Rho-associated coiled-coil kinase ROCK occurs at residues Thr697 and Thr855. cAMP-dependent protein kinase phosphorylates these two sites and the neighboring Ser696 and Ser854. Prior phosphorylation at Thr697 and Thr855 by ROCK precludes phosphorylation at Ser696 and Ser854 by cAMP-dependent protein kinase. Phosphorylation at Thr697 and Thr855 by ROCK exposes two other sites of phosphorylation by cAMP-dependent protein kinase
phosphoprotein
-
large subunit MYPT1: phosphorylation site Thr-695, potential site for phosphorylation by protein kinase A is Thr-853
phosphoprotein
-
myosin light chain phosphatase is regulated by phosphorylation of the catalytic subunit
phosphoprotein
MYPT1 is cleaved by caspase-3 at Asp-884 in apoptotic cells, and the cleaved MYPT1 is strongly phosphorylated at Thr-696 and Thr-853, phosphorylation of which is known to inhibit myosin II binding
phosphoprotein
selective thiophosphorylation of MYPT1 at Thr696 with ROCK inhibits the MLCP activity 30%, whereas the Thr853 thio-phosphorylation does not alter the phosphatase activity. Both Thr696 and Thr853 sites undergo autodephosphorylation
phosphoprotein
-
regulatory subunit of enzmye is phopshorylated at T696, contraction of intact mouse arteries induced with noradrenaline is associated with a 2fold increase in phosphorylation, which is reversed in arteries relaxed with urocortin
phosphoprotein
MYPT1 is cleaved by caspase-3 at Asp-884 in apoptotic cells, and the cleaved MYPT1 is strongly phosphorylated at Thr-696 and Thr-853, phosphorylation of which is known to inhibit myosin II binding
phosphoprotein
phosphorylation of MYPT1 residue T694 is a primary mechanism contributing to inhibition of myosin light chain phosphatase activity and enhancement of myosin regulatory light chain phosphorylation in vivo
phosphoprotein
-
phosphorylation of the myosin-binding subunit of MLCP at the inhibitory site Thr-641 inhibits MLCP activity, but may not play a significant role in a mechanism for MLCP regulation, Rho kinase phosphorylates Thr-799, but not Thr-641
phosphoprotein
-
phosphorylation at Thr-695 of the MLCP regulatory subunit MYPT1 inhibits MLCP activity, Thr-695 phosphorylation is independent of stimulation of G-proteins, Rho-kinase or protein kinase C, MYPT1 can also be phosphorylated at Thr-850, which is a non-inhibitory Rho-kinase site, Thr-850 phosphorylation is activated by G-proteins
phosphoprotein
-
myosin-binding subunit of MLCP is phosphorylated at Thr-641 and Thr-799 by Rho kinase to 2 mol phosphate/mol of MBS
phosphoprotein
-
phosphorylation of MYPT1 is a major mechanism of MLCP regulation. Two major ROK phosphorylation sites, Thr697 and Thr855, on MYPT1 elicit MLCP inhibition. Phosphorylation of both sites inhibits MLCP activity. MYPT1-T855 phosphorylation may also interfere with the binding of MYPT1 to myosin
phosphoprotein
-
treatment of Triton-skinned rat caudal arterial smooth muscle strips with the membrane-impermeant phosphatase inhibitor microcystin or treatment of intact tissue with the membrane-permeant phosphatase inhibitor calyculin A induces slow, sustained contractions that correlate with phosphorylation of MYPT1 at 7 to more than 10 sites
phosphoprotein
-
Ca2+-desensitizing hypoxic relaxation requires dephosphorylation of myosin phosphatase regulatory subunit
proteolytic modification
in apoptotic cells, the myosin-binding domain of myosin phosphatase targeting subunit 1 (MYPT1) is cleaved by caspase-3 at Asp-884
proteolytic modification
in apoptotic cells, the myosin-binding domain of myosin phosphatase targeting subunit 1 (MYPT1) is cleaved by caspase-3 at Asp-884
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
determination of three-dimensional structure of the 57-residue peptide corresponding to residue 658-714 of myosin phosphatase targeting subunit 1 using multi-dimensional NMR techniques
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DELTA495-1030
using a deletion mutant it is shown that the C-terminal domain of human MYPT1(495-1030) is responsible for the binding to the N-terminal portion of myosin light meromyosin
F38A
-
site-directed mutagenesis of subunit MYPT1, the mutant subunit is unable to bind to subunit PP1cbeta
G280A
-
site-directed mutagenesis of subunit PP1cbeta, the mutation does not affect interaction with MYPT1
H237N/K238R
-
site-directed mutagenesis of subunit PP1cgamma, the mutant subunit shows over 90% reduced ability to bind to subunit MYPT1
N236H/R237K
-
site-directed mutagenesis of subunit PP1cbeta, the mutation does not affect interaction with MYPT1
Q198T
-
site-directed mutagenesis of subunit PP1cgamma, mutant subunit is unable to bind to subunit MYPT1
S232A
-
site-directed mutagenesis of subunit PP1cbeta, the mutation does not affect interaction with MYPT1
T197Q
-
site-directed mutagenesis of subunit PP1cbeta, the mutant subunit is unable to bind to subunit MYPT1
T696A
substitution of Thr696 with Ala eliminates the phosphorylation-dependent inhibition
T853A
the extent of inhibition of mutant T853A MLCP is indistinguishable from that of wild-type
additional information
additional information
-
various truncation mutants of the 130 kDa subunit M130
additional information
-
overexpression of full-length enzyme in NIH3T3 cells in presence of serum causes a marked decrease in number of attached cells, block in the cell cycle prior to M phase and signs of increased apoptosis
additional information
-
knock down of either or both isoforms of enzyme subunit MYPT 1 results in inhibition of myosin regulatory light chain dephosphorylation, of cell migration and adhesion, and in an increase of F-actin relative to G-actin in HeLa-cells
additional information
-
overexpression of full-length enzyme in NIH3T3 cells in presence of serum causes a marked decrease in number of attached cells, block in the cell cycle prior to M phase and signs of increased apoptosis
additional information
expression of the caspase-3 cleaved form of MYPT1 that lacks the C-terminal end in HeLa cells causes the dissociation of MYPT1 from actin stress fibers
additional information
-
deletion of the C-terminal residues of MYPT1 at codon 39, 172, 297 and 517 by site directed mutagenesis
additional information
-
construction of synthetic segments of MYPT1 (1-19) and (24-41) and MYPT1(1-19) and (24-41) peptides
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, enzyme SMP-I, 20 mM KCl, 20 mM Tris-HCl, pH 7.4, 50% glycerol, 0.5 mM EGTA, 0.5 mM EDTA, 1 mM dithiothreitol, at least 1 year, stable
-
-20°C, enzyme SMP-IV, 20 mM KCl, 20 mM Tris-HCl, pH 7.4, 50% glycerol, 0.1 mM EGTA, 0.1 mM EDTA, 1 mM dithiothreitol, 0.1 mM phenylmethylsulfonyl fluoride, several months, stable
-
-70°C, enzyme SMP-I, 1 M KCl, 20 mM Tris-HCl, pH 7.4, 0.5 mM EGTA, 0.5 mM EDTA, 1 mM dithiothreitol, at least 1 year, stable
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by immunoprecipitation from primary thymocytes using anti-PP1a, anti-PP1b, anti-MYPT1 antibodies in combination with protein A-Sepharose slurry, myosin phosphatase subunits PP1b and MYPT1 coimmunoprecipitate with HDAC7
-
Flag MYPT1 using anti-Flag affinity chromatography, His tagged proteins by Ni-NTA chromatography
-
KAMPPase, copurification of MLCPase and myosin light chain kinase activities, forming a multienzyme complex
-
native enzyme 340fold by ion exchange and hydrophobic interaction chromatography
-
recombinant 130 kDa regulatory myosin-binding subunit, expressed in SF9 cells
-
recombinant 133 kDa myosin-binding subunit and 20 kDa regulatory subunit, expressed in Escherichia coli
-
recombinant heart-specific small regulatory subunit isoforms hHS-M21 A and B of MLCP
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
an 89.6 kDa N-terminal fragment of MYPT1, an isoform of the 130 kDa regulatory targeting subunit of myosin phosphatase, is cloned and sequenced, MYPT is expressed by 2 genes, the two gene classes are termed MYPT1 and MYPT2
cDNAs encoding the 133 kDa myosin-binding subunit and the 20 kDa regulatory subunit are cloned and expressed in Escherichia coli BL21(DE3)
-
cDNAs encoding the 2 isoforms of the 130 kDa myosin binding subunit are cloned and sequenced
-
cDNAs encoding the heart-specific small regulatory subunit isoforms hHS-M21 A and B of MLCP are cloned, sequenced and expressed in Escherichia coli, the small subunit is the product of the same gene as the large subunit: MYPT2, genomic structure of the gene for hHS-M21, the genes MYPT1 and MYPT2 encoding the large myosin-binding subunit MBS are cloned and expressed in Escherichia coli, genomic organisation of the MYPT2 gene, located on chromosome 1q32
cloning of the cDNAs encoding the 130 kDa regulatory myosin-binding subunit MLCPa, the 38 kDa catalytic subunit MLCPc and the 20 kDa regulatory subunit MLCPsr, the full-length 130 kDa subunit is expressed in SF9 insect cells using the baculovirus expression system and sequenced
-
co-expression of each of two myc-tagged myosin PPase targeting subunit 1 (MYPT1) isozymes with HA-tagged MLC phosphatase catalytic subunit CS1beta in COS-7 cells, and co-expression with ERM proteins ezrin, radixin, and moesin in COS-7 cells
-
expression in DO11/10 T cells, downregulation of myosin phosphatase genes by using siRNA for PP1 isoforms and MYPT1
-
expression of FLAG-tagged full-length catalytic subunit MYPT1 in COS-7 cells, co-expression with Rho-associated kinase
-
expression of wild-type and mutant enzymes in CHO cells using a retroviral vector
-
His-tagged 57-residue peptide corresponding to residue 658-714 of myosin phosphatase targeting subunit 1 expressed in Escherichia coli
in Escherichia coli, expression of various C-terminal MYPT1 peptides bearing various combinations of a predicted coiled coil region, extensions preceding this coiled coil region, and the leucine-zipper motif
-
of MYPT1 in yeast AH109 strain for yeast two hybrid screening, MLCP holoenzyme in Sf9 cells by coinfection of rat His MYPT1, Flag MYPT1, rat PP1delta, and rat M21 expressing viruses, transfection of COS7 or NIH3T3 cells
-
overexpression of MYPT1 and MYPT2 in primary cultures of cardiac myocytes and in COS7 cells using baculoviral and adenoviral expression systems
-
several isoforms of the large targeting subunit MYPT are encoded by 2 genes: MYPT1 and MYPT2, located on chromosomes 12 and 1, structure of MYPT1, MYPT2 is cloned from brain
-
the 18.5 kDa isoform of the small subunit of MP is cloned and expressed in Escherichia coli KS1000(DE3)
-
the lethal mutation FP41 is a missense mutation changing one of the six highly conserved residues in the catalytic domain, D222N in flw-PA and D91N in flw-PB, it is mapped by meiotic recombination with visible recessive markers to the region between cut (7B4) and vermilion (9F11) and between P-elements PBac(WH)CG34408f03664 (9B7) and PBac(WH)Neb-cGPf02352 (9C4), sequence determination of the wild-type and mutant gene from genomic DNA from single FP41/Y larvae and controls
-
various parts of myosin phosphatase targeting subunit GST-fusions expressed in Escherichia coli
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
stability of subunits PP1cbeta and MYPT1 is interdependent, knocking down one of the subunits decreases the expression level of the other
-
the expression of isovariants PPP1R12A, PPP1R12BLZ+, PPP1R16A and PPP1R16B mRNA is reduced in late pregnancy (not-in-labor) relative to non-pregnancy. PPP1R12ALZ+ and PPP1R12ALZ- mRNA levels are similar in the non-pregnant and pregnant not-in-labor groups. There is a further reduction in the uterine expression of PPP1R12ALZ+, PPP1R12CLZ+ and PPP1R12ALZ- mRNA with labor relative to the pregnant not-in-labor group. PPP1R12A, PPP1R12BLZ+, PPP1R16A and PPP1R16B mRNA levels are invariant between the not in labor and in-labor groups
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
additional information
medicine
-
Ca2+-desensitizing hypoxic relaxation requires dephosphorylation of myosin phosphatase regulatory subunit
medicine
-
in response to portal hypertension, abundance of MYPT 1 subunit is significantly reduced and switches to the leucine-zipper positive isoform
medicine
-
upon induction of congestive heart failure, left ventricular function is reduced to about 30% with concomitant decrease in sensitivity to 8-Br-+cGMP and expression of leucine-zipper positive isoform of MYPT 1 subunit
medicine
-
DMBS maintains epithelial integrity, loss of DMBS causes cell shape changes, loss of localization of the apical markers cadherin and increased accumulations of phospho-myosin regulatory light chain and F-actin, DMBS regulates the reorganization of cytoskeleton through down-regulation of myosin II, DMBS fits many of the criteria for a potential neoplastic type tumor suppressor gene
medicine
-
myosin light chain phosphatase pathway is critical in regulating in vivo myofibroblast differentiation during wound healing and fibrocontractive diseases
medicine
-
MYPT1 is downregulated and switches to the splice variant isoform that codes for the COOH-terminal leucine zipper motif in the hypertension of pregnancy model. These changes in MP expression are prevented by treatment with the antihypertensive medicine hydralazine. Early and effective treatment of hypertension during pregnancy may be able to reverse some of the adverse effects on uterine perfusion and fetal development in this disease
medicine
-
congestive heart failure is associated with a decrease in the COOH-terminus leucine zipper and the myosin targeting subunit of MLPC expression
medicine
the expression of isovariants PPP1R12A, PPP1R12BLZ+, PPP1R16A and PPP1R16B mRNA is reduced in late pregnancy (not-in-labor) relative to non-pregnancy. PPP1R12ALZ+ and PPP1R12ALZ- mRNA levels are similar in the non-pregnant and pregnant not-in-labor groups. There is a further reduction in the uterine expression of PPP1R12ALZ+, PPP1R12CLZ+ and PPP1R12ALZ- mRNA with labor relative to the pregnant not-in-labor group. PPP1R12A, PPP1R12BLZ+, PPP1R16A and PPP1R16B mRNA levels are invariant between the not in labor and in-labor groups
medicine
-
myosin light chain phosphatase pathway is critical in regulating in vivo myofibroblast differentiation during wound healing and fibrocontractive diseases
-
additional information
-
dephosphorylation of myosin regulatory light-chain is essential for rapid recruitment or assembly of myosin II filaments, myosin phosphatase localizes to stress fibers depending on the activity of myosin II ATPase
additional information
-
phosphorylation of endogenous inhibitor proteins provides a mechanism for reciprocal coordination of kinase and phosphatase activities
additional information
-
dephosphorylation of myosin regulatory light-chain is essential for rapid recruitment or assembly of myosin II filaments, myosin phosphatase localizes to stress fibers depending on the activity of myosin II ATPase
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sobieszek, A.; Borkowski, J.; Babiychuk, V.S.
Purification and characterization of a smooth muscle myosin light chain kinase-phosphatase complex
J. Biol. Chem.
272
7034-7041
1997
Meleagris gallopavo
brenda
Pato, M.D.; Adelstein, R.S.
Purification and characterization of a multisubunit phosphatase from turkey gizzard smooth muscle. The effect of calmodulin binding to myosin light chain kinase on dephosphorylation
J. Biol. Chem.
258
7047-7054
1983
Meleagris gallopavo
brenda
Houston, M.E.; Lingley, M.D.; Stuart, D.S.; Grange, R.W.
Myosin light chain phosphorylation in intact human muscle
FEBS Lett.
219
469-471
1987
Homo sapiens
brenda
Pato, M.D.; Kerc, E.
Purification of smooth muscle myosin phosphatase from turkey gizzard
Methods Enzymol.
159
446-453
1988
Meleagris gallopavo
brenda
Shimizu, H.; Ito, M.; Miyahara, M.; Ichikawa, K.; Okubo, S.; Konishi, T.; Naka, M.; Tanaka, T.; Hirano, K.; Hartshorne, D.J.; Nakano, T.
Characterization of the myosin-binding subunit of smooth muscle myosin phosphatase
J. Biol. Chem.
269
30407-30411
1994
Gallus gallus
brenda
Chisholm, A.A.K.; Cohen, P.
The myosin-bound form of protein phosphatase 1 (PP-1M) is the enzyme that dephosphorylates native myosin in skeletal and cardiac muscles
Biochim. Biophys. Acta
971
163-169
1988
Bos taurus, Oryctolagus cuniculus
brenda
Alessi, D.; MacDougall, L.K.; Sola, M.M.; Ikebe, M.; Cohen, P.
The control of protein phosphatase-1 by targetting subunits. The major myosin phosphatase in avian smooth muscle is a novel form of protein phosphatase-1
Eur. J. Biochem.
210
1023-1035
1992
Gallus gallus, Gallus gallus PP-1
brenda
Sato, O.; Ogawa, Y.
Myosin assembly critical for the enzyme activity of smooth muscle myosin phosphatase: Effects of MgATP, ionic strength, and Mg2+
J. Biochem.
129
881-889
2001
Gallus gallus
brenda
Hirano, M.; Niiro, N.; Hirano, K.; Nishimura, J.; Hartshorne, D.J.; Kanaide, H.
Expression, subcellular localization, and cloning of the 130-kDa regulatory subunit of myosin phosphatase in porcine aortic endothelial cells
Biochem. Biophys. Res. Commun.
254
490-496
1999
Sus scrofa (Q9TV77), Sus scrofa
brenda
Zhang, Y.; Mabuchi, K.; Tao, T.
Expression in insect cells and characterization of the 110 kDa anchoring subunit of myosin light chain phosphatase
Biochim. Biophys. Acta
1343
51-58
1997
Gallus gallus, Gallus gallus MLCP
brenda
Schmidt, U.S.; Troschka, M.; Pfitzer, G.
The variable coupling between force and myosin light chain phosphorylation in Triton-skinned chicken gizzard fibre bundles: Role of myosin light chain phosphatase
Pflugers Arch.
429
708-715
1995
Gallus gallus
brenda
Kitazawa, T.; Eto, M.; Woodsome, T.P.; Khalequzzaman, M.
Phosphorylation of the myosin phosphatase targeting subunit and CPI-17 during Ca2+ sensitization in rabbit smooth muscle
J. Physiol.
546
879-889
2003
Oryctolagus cuniculus
brenda
Ito, M.; Feng, J.; Tsujino, S.; Inagaki, N.; Inagaki, M.; Tanaka, J.; Ichikawa, K.; Hartshorne, D.J.; Nakano, T.
Interaction of smooth muscle myosin phosphatase with phospholipids
Biochemistry
36
7607-7614
1997
Gallus gallus, Rattus norvegicus
brenda
Gailly, P.; Wu, X.; Haystead, T.A.J.; Somlyo, A.P.; Cohen, P.T.W.; Cohen, P.; Somlyo, A.V.
Regions of the 110-kDa regulatory subunit M110 required for regulation of myosin-light-chain-phosphatase activity in smooth muscle
Eur. J. Biochem.
239
326-332
1996
Rattus norvegicus, Sus scrofa, Sus scrofa SMPP-1M
brenda
Belik, J.; Majumdar, R.; Fabris, V.E.; Kerc, E.; Pato, M.D.
Myosin light chain phosphatase and kinase abnormalities in fetal sheep pulmonary hypertension
Pediatr. Res.
43
57-61
1998
Ovis aries
brenda
Richards, C.T.; Ogut, O.; Brozovich, F.V.
Agonist-induced force enhancement. The role of isoforms and phosphorylation of the myosin-targeting subunit of myosin light chain phosphatase
J. Biol. Chem.
277
4422-4427
2002
Gallus gallus
brenda
Langsetmo, K.; Stafford, W.F., 3rd; Mabuchi, K.; Tao, T.
Recombinant small subunit of smooth muscle myosin light chain phosphatase. Molecular properties and interactions with the targeting subunit
J. Biol. Chem.
276
34318-34322
2001
Gallus gallus, Gallus gallus PP-1M
brenda
Etter, E.F.; Eto, M.; Wardle, R.L.; Brautigan, D.L.; Murphy, R.A.
Activation of myosin light chain phosphatase in intact arterial smooth muscle during nitric oxide-induced relaxation
J. Biol. Chem.
276
34681-34685
2001
Sus scrofa
brenda
Ikebe, R.; Reardon, S.; Mitsui, T.; Ikebe, M.
Role of the N-terminal region of the regulatory light chain in the dephosphorylation of myosin by myosin light chain phosphatase
J. Biol. Chem.
274
30122-30126
1999
Meleagris gallopavo, Meleagris gallopavo MLCP
brenda
Muranyi, A.; Erdodi, F.; Ito, M.; Gergely, P.; Hartshorne, D.J.
Identification and localization of myosin phosphatase in human platelets
Biochem. J.
330
225-231
1998
Homo sapiens
-
brenda
Niiro, N.; Koga, Y.; Ikebe, M.
Agonist-induced changes in the phosphorylation of the myosin-binding subunit of myosin light chain phosphatase and CPI17, two regulatory factors of myosin light chain phosphatase, in smooth muscle
Biochem. J.
369
117-128
2003
Oryctolagus cuniculus, Rattus norvegicus
brenda
Essler, M.; Amano, M.; Kruse, H.J.; Kaibuchi, K.; Weber, P.C.; Aepfelbacher, M.
Thrombin inactivates myosin light chain phosphatase via Rho and its target Rho kinase in human endothelial cells
J. Biol. Chem.
273
21867-21874
1998
Homo sapiens
brenda
Hirano, K.; Phan, B.C.; Hartshorne, D.J.
Interactions of the subunits of smooth muscle myosin phosphatase
J. Biol. Chem.
272
3683-3688
1997
Gallus gallus, Meleagris gallopavo
brenda
Arimura, T.; Suematsu, N.; Zhou, Y.B.; Nishimura, J.; Satoh, S.; Takeshita, A.; Kanaide, H.; Kimura, A.
Identification, characterization, and functional analysis of heart-specific myosin light chain phosphatase small subunit
J. Biol. Chem.
276
6073-6082
2001
Homo sapiens (O60237)
brenda
Parizi, M.; Howard, E.W.; Tomasek, J.J.
Regulation of LPA-promoted myofibroblast contraction: Role of Rho, myosin light chain kinase, and myosin light chain phosphatase
Exp. Cell Res.
254
210-220
2000
Homo sapiens
brenda
Hartshorne, D.J.
Myosin phosphatase: Subunits and interactions
Acta Physiol. Scand.
164
483-493
1998
Gallus gallus, Homo sapiens
brenda
Payne, M.C.; Zhang, H.Y.; Shirasawa, Y.; Koga, Y.; Ikebe, M.; Benoit, J.N.; Fisher, S.A.
Dynamic changes in expression of myosin phosphatase in a model of portal hypertension
Am. J. Physiol.
286
H1801-H1810
2004
Rattus norvegicus
brenda
Belik, J.; Kerc, E.; Pato, M.D.
Rat pulmonary arterial smooth muscle myosin light chain kinase and phosphatase activities decrease with age
Am. J. Physiol.
290
L509-516
2006
Rattus norvegicus
brenda
Karim, S.M.; Rhee, A.Y.; Given, A.M.; Faulx, M.D.; Hoit, B.D.; Brozovich, F.V.
Vascular reactivity in heart failure: role of myosin light chain phosphatase
Circ. Res.
95
612-618
2004
Rattus norvegicus
brenda
Lubomirov, L.T.; Reimann, K.; Metzler, D.; Hasse, V.; Stehle, R.; Ito, M.; Hartshorne, D.J.; Gagov, H.; Pfitzer, G.; Schubert, R.
Urocortin-induced decrease in Ca2+ sensitivity of contraction in mouse tail arteries is attributable to cAMP-dependent dephosphorylation of MYPT1 and activation of myosin light chain phosphatase
Circ. Res.
98
1159-1167
2006
Mus musculus
brenda
Xia, D.; Stull, J.T.; Kamm, K.E.
Myosin phosphatase targeting subunit 1 affects cell migration by regulating myosin phosphorylation and actin assembly
Exp. Cell Res.
304
506-517
2005
Homo sapiens
brenda
Goeckeler, Z.M.; Wysolmerski, R.B.
Myosin phosphatase and cofilin mediate cAMP/cAMP-dependent protein kinase-induced decline in endothelial cell isometric tension and myosin II regulatory light chain phosphorylation
J. Biol. Chem.
280
33083-33095
2005
Bos taurus
brenda
Koga, Y.; Ikebe, M.
p116Rip decreases myosin II phosphorylation by activating myosin light chain phosphatase and by inactivating RhoA
J. Biol. Chem.
280
4983-4991
2005
Rattus norvegicus
brenda
Lontay, B.; Serfozo, Z.; Gergely, P.; Ito, M.; Hartshorne, D.J.; Erdodi, F.
Localization of myosin phosphatase target subunit 1 in rat brain and in primary cultures of neuronal cells
J. Comp. Neurol.
478
72-87
2004
Rattus norvegicus
brenda
Payne, M.C.; Zhang, H.Y.; Prosdocimo, T.; Joyce, K.M.; Koga, Y.; Ikebe, M.; Fisher, S.A.
Myosin phosphatase isoform switching in vascular smooth muscle development
J. Mol. Cell. Cardiol.
40
274-282
2006
Rattus norvegicus
brenda
Wu, Y.; Muranyi, A.; Erdodi, F.; Hartshorne, D.J.
Localization of myosin phosphatase target subunit and its mutants
J. Muscle Res. Cell Motil.
26
123-134
2005
Gallus gallus, Homo sapiens
brenda
Wardle, R.L.; Gu, M.; Ishida, Y.; Paul, R.J.
Ca2+-desensitizing hypoxic vasorelaxation: pivotal role for the myosin binding subunit of myosin phosphatase (MYPT1) in porcine coronary artery
J. Physiol.
572
259-267
2006
Sus scrofa
brenda
Lu, Y.; Zhang, H.; Gokina, N.I.; Mandala, M.; Sato, O.; Ikebe, M.; Osol, G.; Fisher, S.A.
Uterine artery myosin phosphatase isoform switching and increased sensitivity to SNP in a rat L-NAME model of hypertension of pregnancy
Am. J. Physiol. Cell Physiol.
294
C564-C571
2008
Rattus norvegicus
brenda
Matsumura, F.; Hartshorne, D.J.
Myosin phosphatase target subunit: Many roles in cell function
Biochem. Biophys. Res. Commun.
369
149-56
2007
Mammalia
brenda
Okamoto, R.; Kato, T.; Mizoguchi, A.; Takahashi, N.; Nakakuki, T.; Mizutani, H.; Isaka, N.; Imanaka-Yoshida, K.; Kaibuchi, K.; Lu, Z.; Mabuchi, K.; Tao, T.; Hartshorne, D.J.; Nakano, T.; Ito, M.
Characterization and function of MYPT2, a target subunit of myosin phosphatase in heart
Cell. Signal.
18
1408-1416
2006
Mammalia
brenda
Jeon, S.B.; Kim, G.; Kim, J.I.; Seok, Y.M.; Kim, S.H.; Suk, K.; Shin, H.M.; Lee, Y.H.; Kim, I.K.
Flavone inhibits vascular contraction by decreasing phosphorylation of the myosin phosphatase target subunit
Clin. Exp. Pharmacol. Physiol.
34
1116-1120
2007
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
brenda
Mitonaka, T.; Muramatsu, Y.; Sugiyama, S.; Mizuno, T.; Nishida, Y.
Essential roles of myosin phosphatase in the maintenance of epithelial cell integrity of Drosophila imaginal disc cells
Dev. Biol.
309
78-86
2007
Drosophila melanogaster
brenda
Parra, M.; Mahmoudi, T.; Verdin, E.
Myosin phosphatase dephosphorylates HDAC7, controls its nucleocytoplasmic shuttling, and inhibits apoptosis in thymocytes
Genes Dev.
21
638-643
2007
Mus musculus, Mus musculus BALB/c
brenda
Kirchner, J.; Gross, S.; Bennett, D.; Alphey, L.
The nonmuscle myosin phosphatase PP1beta (flapwing) negatively regulates Jun N-terminal kinase in wing imaginal discs of Drosophila
Genetics
175
1741-1749
2007
Drosophila melanogaster
brenda
Lee, E.; Hayes, D.B.; Langsetmo, K.; Sundberg, E.J.; Tao, T.C.
Interactions between the leucine-zipper motif of cGMP-dependent protein kinase and the C-terminal region of the targeting subunit of myosin light chain phosphatase
J. Mol. Biol.
373
1198-1212
2007
Homo sapiens
brenda
Azam, M.A.; Yoshioka, K.; Ohkura, S.; Takuwa, N.; Sugimoto, N.; Sato, K.; Takuwa, Y.
Ca2+-independent, inhibitory effects of cyclic adenosine 5-monophosphate on Ca2+ regulation of phosphoinositide 3-kinase C2alpha, Rho, and myosin phosphatase in vascular smooth muscle
J. Pharmacol. Exp. Ther.
320
907-916
2007
Oryctolagus cuniculus
brenda
Watanabe, T.; Hosoya, H.; Yonemura, S.
Regulation of myosin II dynamics by phosphorylation and dephosphorylation of its light chain in epithelial cells
Mol. Biol. Cell
18
605-616
2007
Canis lupus familiaris, Canis lupus familiaris Madin Darby
brenda
Koga, Y.; Ikebe, M.
A novel regulatory mechanism of myosin light chain phosphorylation via binding of 14-3-3 to myosin phosphatase
Mol. Biol. Cell
19
1062-1071
2007
Rattus norvegicus
brenda
Eto, M.; Kitazawa, T.; Matsuzawa, F.; Aikawa, S.; Kirkbride, J.A.; Isozumi, N.; Nishimura, Y.; Brautigan, D.L.; Ohki, S.
Phosphorylation-induced conformational switching of CPI-17 produces a potent myosin phosphatase inhibitor
Structure
15
1591-1602
2007
Sus scrofa
brenda
Tomasek, J.J.; Vaughan, M.B.; Kropp, B.P.; Gabbiani, G.; Martin, M.D.; Haaksma, C.J.; Hinz, B.
Contraction of myofibroblasts in granulation tissue is dependent on Rho/Rho kinase/myosin light chain phosphatase activity
Wound Repair Regen.
14
313-320
2006
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
brenda
Mizuno, Y.; Isotani, E.; Huang, J.; Ding, H.; Stull, J.T.; Kamm, K.E.
Myosin light chain kinase activation and calcium sensitization in smooth muscle in vivo
Am. J. Physiol. Cell Physiol.
295
C358-C364
2008
Homo sapiens
brenda
Sharma, A.K.; Zhou, G.P.; Kupferman, J.; Surks, H.K.; Christensen, E.N.; Chou, J.J.; Mendelsohn, M.E.; Rigby, A.C.
Probing the interaction between the coiled-coil leucine zipper of cGMP-dependent protein kinase Ialpha and the C-terminus of the myosin binding subunit of the myosin light chain phosphatase
J. Biol. Chem.
283
32860-32869
2008
Homo sapiens
brenda
Wang, Y.; Zheng, X.R.; Riddick, N.; Bryden, M.; Baur, W.; Zhang, X.; Surks, H.K.
ROCK isoform regulation of myosin phosphatase and contractility in vascular smooth muscle cells
Circ. Res.
104
531-540
2009
Rattus norvegicus
brenda
Ogut, O.; Brozovich, F.V.
The potential role of MLC phosphatase and MAPK signalling in the pathogenesis of vascular dysfunction in heart failure
J. Cell. Mol. Med.
12
2158-2164
2008
Homo sapiens
brenda
Ratz, P.H.; Miner, A.S.
Role of protein kinase Czeta and calcium entry in KCl-induced vascular smooth muscle calcium sensitization and feedback control of cellular calcium levels
J. Pharmacol. Exp. Ther.
328
399-408
2009
Oryctolagus cuniculus
brenda
Borman, M.A.; Freed, T.A.; Haystead, T.A.; Macdonald, J.A.
The role of the calponin homology domain of smoothelin-like 1 (SMTNL1) in myosin phosphatase inhibition and smooth muscle contraction
Mol. Cell. Biochem.
327
93-100
2009
Oryctolagus cuniculus
brenda
Webb, J.D.; Muranyi, A.; Pugh, C.W.; Ratcliffe, P.J.; Coleman, M.L.
MYPT1, the targeting subunit of smooth-muscle myosin phosphatase, is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH)
Biochem. J.
420
327-333
2009
Homo sapiens, Meleagris gallopavo
brenda
Kiss, A.; Lontay, B.; Becsi, B.; Markasz, L.; Olah, E.; Gergely, P.; Erdodi, F.
Myosin phosphatase interacts with and dephosphorylates the retinoblastoma protein in THP-1 leukemic cells: its inhibition is involved in the attenuation of daunorubicin-induced cell death by calyculin-A
Cell. Signal.
20
2059-2070
2008
Homo sapiens
brenda
Umeda, D.; Yamada, K.; Tachibana, H.
H89 (N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide) induces reduction of myosin regulatory light chain phosphorylation and inhibits cell proliferation
Eur. J. Pharmacol.
590
61-66
2008
Homo sapiens
brenda
Khromov, A.; Choudhury, N.; Stevenson, A.S.; Somlyo, A.V.; Eto, M.
Phosphorylation-dependent autoinhibition of myosin light chain phosphatase accounts for Ca2+ sensitization force of smooth muscle contraction
J. Biol. Chem.
284
21569-21579
2009
Homo sapiens, Sus scrofa
brenda
Mori, S.; Iwaoka, R.; Eto, M.; Ohki, S.
Solution structure of the inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1
Proteins
77
732-735
2009
Homo sapiens (O14974)
brenda
Cole, W.C.; Welsh, D.G.
Role of myosin light chain kinase and myosin light chain phosphatase in the resistance arterial myogenic response to intravascular pressure
Arch. Biochem. Biophys.
510
160-173
2011
Rattus norvegicus
brenda
Matsumura, F.; Yamakita, Y.; Yamashiro, S.
Myosin light chain kinases and phosphatase in mitosis and cytokinesis
Arch. Biochem. Biophys.
510
76-82
2011
Homo sapiens
brenda
Okada, C.; Nakamura, A.; Tomioka, S.; Kohama, K.; Kaneko, T.S.
Purification and characterization of the plasmodial phosphatase that hydrolyses the phosphorylated light chain of Physarum myosin II from Physarum polycephalum
Cell Biol. Int.
34
827-835
2010
Physarum polycephalum
brenda
Sun, Y.; Yan, Y.; Denef, N.; Schuepbach, T.
Regulation of somatic myosin activity by protein phosphatase 1beta controls Drosophila oocyte polarization
Development
138
1991-2001
2011
Drosophila melanogaster
brenda
Shichi, D.; Arimura, T.; Ishikawa, T.; Kimura, A.
Heart-specific small subunit of myosin light chain phosphatase activates rho-associated kinase and regulates phosphorylation of myosin phosphatase target subunit 1
J. Biol. Chem.
285
33680-33690
2010
Homo sapiens
brenda
Scotto-Lavino, E.; Garcia-Diaz, M.; Du, G.; Frohman, M.A.
Basis for the isoform-specific interaction of myosin phosphatase subunits protein phosphatase 1c beta and myosin phosphatase targeting subunit 1
J. Biol. Chem.
285
6419-6424
2010
Homo sapiens
brenda
Kim, K.M.; Csortos, C.; Czikora, I.; Fulton, D.; Umapathy, N.S.; Olah, G.; Verin, A.D.
Molecular characterization of myosin phosphatase in endothelium
J. Cell. Physiol.
227
1701-1708
2012
Homo sapiens
brenda
Lee, J.H.; Palaia, T.; Ragolia, L.
Impaired insulin-stimulated myosin phosphatase Rho-interacting protein signaling in diabetic Goto-Kakizaki vascular smooth muscle cells
Am. J. Physiol. Cell Physiol.
302
C1371-C1381
2012
Rattus norvegicus
brenda
Khasnis, M.; Nakatomi, A.; Gumpper, K.; Eto, M.
Reconstituted human myosin light chain phosphatase reveals distinct roles of two inhibitory phosphorylation sites of the regulatory subunit, MYPT1
Biochemistry
53
2701-2709
2014
Homo sapiens (O14974), Homo sapiens
brenda
Ryan, T.; Shelton, M.; Lambert, J.P.; Malecova, B.; Boisvenue, S.; Ruel, M.; Figeys, D.; Puri, P.L.; Skerjanc, I.S.
Myosin phosphatase modulates the cardiac cell fate by regulating the subcellular localization of Nkx2.5 in a Wnt/Rho-associated protein kinase-dependent pathway
Circ. Res.
112
257-266
2013
Homo sapiens
brenda
Majumder, P.; Aranjuez, G.; Amick, J.; McDonald, J.A.
Par-1 controls myosin-II activity through myosin phosphatase to regulate border cell migration
Curr. Biol.
22
363-372
2012
Drosophila melanogaster
brenda
Qiao, Y.N.; He, W.Q.; Chen, C.P.; Zhang, C.H.; Zhao, W.; Wang, P.; Zhang, L.; Wu, Y.Z.; Yang, X.; Peng, Y.J.; Gao, J.M.; Kamm, K.E.; Stull, J.T.; Zhu, M.S.
Myosin phosphatase target subunit 1 (MYPT1) regulates the contraction and relaxation of vascular smooth muscle and maintains blood pressure
J. Biol. Chem.
289
22512-22523
2014
Mus musculus (Q9DBR7)
brenda
Iwasaki, T.; Katayama, T.; Kohama, K.; Endo, Y.; Sawasaki, T.
Myosin phosphatase is inactivated by caspase-3 cleavage and phosphorylation of myosin phosphatase targeting subunit 1 during apoptosis
Mol. Biol. Cell
24
748-756
2013
Homo sapiens (O14974), Mus musculus (Q9DBR7)
brenda
Jayashankar, V.; Nguyen, M.J.; Carr, B.W.; Zheng, D.C.; Rosales, J.B.; Rosales, J.B.; Weiser, D.C.
Protein phosphatase 1 beta paralogs encode the zebrafish myosin phosphatase catalytic subunit
PLoS ONE
8
e75766
2013
Danio rerio
brenda
Sutherland, C.; MacDonald, J.A.; Walsh, M.P.
Analysis of phosphorylation of the myosin-targeting subunit of myosin light chain phosphatase by Phos-tag SDS-PAGE
Am. J. Physiol. Cell Physiol.
310
C681-C691
2016
Rattus norvegicus, Gallus gallus (Q90623)
brenda
Reho, J.J.; Kenchegowda, D.; Asico, L.D.; Fisher, S.A.
A splice variant of the myosin phosphatase regulatory subunit tunes arterial reactivity and suppresses response to salt loading
Am. J. Physiol. Heart Circ. Physiol.
310
H1715-H1724
2016
Mus musculus (Q9DBR7)
brenda
Arimura, T.; Muchir, A.; Kuwahara, M.; Morimoto, S.; Ishikawa, T.; Du, C.K.; Zhan, D.Y.; Nakao, S.; Machida, N.; Tanaka, R.; Yamane, Y.; Hayashi, T.; Kimura, A.
Overexpression of heart-specific small subunit of myosin light chain phosphatase results in heart failure and conduction disturbance
Am. J. Physiol. Heart Circ. Physiol.
314
H1192-H1202
2018
Mus musculus
brenda
Horvath, D.; Sipos, A.; Major, E.; Konya, Z.; Batori, R.; Dedinszki, D.; Szoell Si, A.; Tamas, I.; Ivan, J.; Kiss, A.; Erd di, F.; Lontay, B.
Myosin phosphatase accelerates cutaneous wound healing by regulating migration and differentiation of epidermal keratinocytes via Akt signaling pathway in human and murine skin
Biochim. Biophys. Acta
1864
3268-3280
2018
Homo sapiens (O14974), Homo sapiens, Mus musculus (Q9DBR7), Mus musculus
brenda
Shibata, K.; Sakai, H.; Huang, Q.; Kamata, H.; Chiba, Y.; Misawa, M.; Ikebe, R.; Ikebe, M.
Rac1 regulates myosin II phosphorylation through regulation of myosin light chain phosphatase
J. Cell. Physiol.
230
1352-1364
2015
Rattus norvegicus (Q10728)
brenda
Chen, C.; Chen, X.; Qiao, Y.; Wang, P.; He, W.; Zhang, C.; Zhao, W.; Gao, Y.; Chen, C.; Tao, T.; Sun, J.; Wang, Y.; Gao, N.; Kamm, K.; Stull, J.; Zhu, M.
In vivo roles for myosin phosphatase targeting subunit-1 phosphorylation sites T694 and T852 in bladder smooth muscle contraction
J. Physiol.
593
681-700
2015
Mus musculus (Q9DBR7), Mus musculus
brenda
Zheng, X.; Heaps, C.; Fisher, S.
Myosin phosphatase isoforms and related transcripts in the pig coronary circulation and effects of exercise and chronic occlusion
Microvasc. Res.
98
166-171
2015
Sus scrofa
brenda
Valencia-Exposito, A.; Grosheva, I.; Miguez, D.G.; Gonzalez-Reyes, A.; Martin-Bermudo, M.D.
Myosin light-chain phosphatase regulates basal actomyosin oscillations during morphogenesis
Nat. Commun.
7
10746
2016
Drosophila melanogaster
brenda
Bremer, J.; Granato, M.
Myosin phosphatase fine-tunes zebrafish motoneuron position during axonogenesis
PLoS Genet.
12
e1006440
2016
Danio rerio (Z4YIS0)
-
brenda
Lee, E.; Stafford, W.3.
Interaction of myosin phosphatase target subunit (MYPT1) with myosin phosphatase-RhoA interacting protein (MRIP) a role of glutamic acids in the interaction
PLoS One
10
e0139875
2015
Homo sapiens (O14974)
brenda
Lartey, J.; Taggart, J.; Robson, S.; Taggart, M.
Altered expression of human smooth muscle myosin phosphatase targeting (MYPT) isovariants with pregnancy and labor
PLoS ONE
11
e0164352
2016
Homo sapiens (O14974), Homo sapiens
brenda
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