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Information on EC 3.1.3.53 - [myosin-light-chain] phosphatase and Organism(s) Homo sapiens
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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 taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
MLCP
MLCPase
-
-
-
-
MLCPPase
-
-
-
-
MP
-
-
-
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myosin light chain kinase phosphatase
-
-
-
-
myosin light chain phosphatase
myosin phosphatase
MYPT1
phosphatase, myosin
-
-
-
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phosphatase, myosin light-chain kinase
-
-
-
-
PP-1G
-
-
-
-
PP-1M
-
-
-
-
PP-2A
-
-
-
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protein phosphatase 2A
-
-
-
-
SMMP
-
-
-
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smooth muscle myosin phosphatase
-
-
-
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smooth muscle phosphatase I-IV
-
-
-
-
SMP-I
-
-
-
-
SMP-II
-
-
-
-
SMP-III
-
-
-
-
SMP-IV
-
-
-
-
SMPP
-
-
-
-
MLCP
-
-
-
-
myosin light chain phosphatase
-
-
-
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myosin phosphatase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
hydrolysis of phosphoric ester
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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.
CAS REGISTRY NUMBER
COMMENTARY
108658-39-5
-
86417-96-1
-
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 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
-
-
?
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
-
-
?
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
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+
-
?
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
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
okadaic acid
-
more potent inhibitor of type 2A phosphatase than of type 1 phosphatase
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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
dephosphorylation activity of myosin phosphatase immunoprecipitated from the apoptotic cells is lower than that from nonapoptotic control cells
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
heart-specific small regulatory subunit isoform hHS-M21 A of MLCP
SwissProt
heart-specific small regulatory subunit isoform hHS-M21 B of MLCP
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
the small regulatory subunit hHS-M21 is expressed only in cardiac muscle, not in smooth muscle
-
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
additional information
expression profiles of the heart-specific small subunit hHS-M21 and of the large myosin-binding subunit of MLCP
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
-
localization of PP-1 and PP-2A and their subunits in platelets
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
additional information
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
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
-
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
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
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
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
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_HUMAN
327
0
37187
Swiss-Prot
other Location (Reliability: 2)
MYPT2_HUMAN
982
0
110404
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
trimer
additional information
trimer
-
myosin light chain phosphatase consists of a catalytic subunit, a large subunit, MYPT1 or MYPT2, and a small subunit
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
proteolytic modification
in apoptotic cells, the myosin-binding domain of myosin phosphatase targeting subunit 1 (MYPT1) is cleaved by caspase-3 at Asp-884
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
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
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
-
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant heart-specific small regulatory subunit isoforms hHS-M21 A and B of MLCP
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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 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
-
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
-
various parts of myosin phosphatase targeting subunit GST-fusions expressed in Escherichia coli
-
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
-
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
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)
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
Hartshorne, D.J.
Myosin phosphatase: Subunits and interactions
Acta Physiol. Scand.
164
483-493
1998
Gallus gallus, Homo sapiens
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
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
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
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
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
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
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
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
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
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
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)
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
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
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
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
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
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
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)
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
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)
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