Any feedback?
Information on EC 5.6.1.1 - microtubule-severing ATPase
for references in articles please use BRENDA:EC5.6.1.1Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
5.6.1.1 microtubule-severing ATPaseIUBMB Comments
A member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome.
Specify your search results
Word Map
- 5.6.1.1
- spastic
- hereditary
- kinesins
- paraplegia
-
mitotic
- cortical
- cytoskeleton
-
disassembly
- centrosome
- gelsolin
-
corticospinal
- atpases
- cytokine
- paraparesis
-
atlastin
-
microtubule-based
-
actin-binding
-
microtubule-binding
-
escrt-iii
-
antimitotic
-
axonopathy
-
minus-ends
- gamma-tubulin
-
kinesin-related
-
plus-ends
-
mt-associated
-
microtubule-dependent
-
phragmoplasts
- midbody
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
n
+
n
+
a microtubule
=
n
+
n
+
(n+1)
alpha/beta tubulin heterodimers
Synonyms
spastin, katanin, scinderin, kinesin spindle protein, mei-1, adseverin, katanin p60, microtubule-severing protein, microtubule-stimulated atpase, p60-katanin, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Arabidopsis thaliana katanin small subunit
-
AtKSS, p60 homolog in plants
AtKSS
katanin catalytic subunit, microtubule-stimulated ATPase activity
EC 3.6.4.3
-
-
formerly
-
katanin
KATANIN 1
katanin p60
mei-1
microtubule severing protein
microtubule-severing ATPase
microtubule-severing protein
p60 KAT1p
P60-katanin
SPAS-1
spastin
SPG4
katanin
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers
n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers
another member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome
-
n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers
another member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome
-
n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers
another member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome
Drosophila sp. (in: flies)
-
n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers
another member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome
-
n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers
another member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome
-
n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers
another member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome
-
n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers
another member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome
-
n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers
another member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome
-
n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers
another member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome
-
n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers
another member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome
-
n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers
another member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome
-
n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers
another member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome
-
n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers
another member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome
Actinocoryne sp.
-
n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers
another member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome
-
n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers
another member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome
n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers
model of enzyme activity based on defect-containing microtubules
-
n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers
Dm-Kat60 severs and depolymerizes microtubules from their ends
-
n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
hydrolysis of phosphoric ester
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (tubulin-dimerizing)
A member of the AAA-ATPase family, active in splitting microtubules into tubulin dimers in the centrosome.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
ATP + H2O
ADP + phosphate
ATP hydrolysis is accompanied by microtubule disassembly
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
recombinant Dm-Kat60 robustly severs taxol-stabilized microtubules in the presence of ATP. This reacton is inhibited when ATP is depleted with hexokinase and glucose or replaced with the non-hydrolysable ATP analogue 5'-adenylyl-beta-gamma-imidotriphosphate AMPPMP
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
binding of either microtuble or C-terminal domain of adaptor-p80 stimulates the ATPase activity of p60-katanin
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O + microtubule
ADP + phosphate + alpha/beta tubulin heterodimers
-
-
-
?
ATP + H2O + microtubule
ADP + phosphate + alpha/beta tubulin heterodimers
assembly of female meiotic spindles requires MEI-1 and MEI-2, which constitute the microtubule-severing AAA+ ATPase Katanin
-
-
?
ATP + H2O + microtubule
ADP + phosphate + alpha/beta tubulin heterodimers
-
-
-
?
ATP + H2O + microtubule
ADP + phosphate + alpha/beta tubulin heterodimers
the microtubule-interacting and trafficking (MIT) domain and adjacent linker region of the Drosophila katanin catalytic subunit Kat60 cooperate to regulate microtubule severing in two distinct ways. First, the MIT domain and linker region of Kat60 decrease its abundance by enhancing its proteasome-dependent degradation. The Drosophila katanin regulatory subunit Kat80, which is required to stabilize Kat60 in cells, conversely reduces the proteasome-dependent degradation of Kat60. Second, the MIT domain and linker region of Kat60 augment its microtubule-disassembly activity by enhancing its association with microtubules
-
-
?
ATP + H2O + microtubule
ADP + phosphate + alpha/beta tubulin heterodimers
-
-
-
?
ATP + H2O + microtubule
ADP + phosphate + alpha/beta tubulin heterodimers
-
-
-
?
ATP + H2O + microtubule
ADP + phosphate + alpha/beta tubulin heterodimers
the enzyme plays important roles in various cellular events including axon regeneration, cytokinesis, and nuclear envelope sealing after mitosis
-
-
?
ATP + H2O + microtubule
ADP + phosphate + alpha/beta tubulin heterodimers
in addition to the AAA domain, the microtubule-binding domain region of spastin is also involved in regulating ATPase activity
-
-
?
ATP + H2O + microtubule
ADP + phosphate + alpha/beta tubulin heterodimers
-
katanin-dependent severing of microtubules is important for proper execution of key cellular activities including cell division, migration, and differentiation
-
-
?
ATP + H2O + microtubule
ADP + phosphate + alpha/beta tubulin heterodimers
-
activity of katanin requires specific domains of both p60 KAT1p catalytic subunit and p80 KAT3p regulatory subunit. In addition to its activating role, p80 can also contribute to the inhibition of p60 KAT1p. Increased levels of tubulin polyglutamylation correlates with a relocalization of p60 KAT1p to glutamylated microtubules, suggesting that binding of katanin subunits to microtubules is regulated differently and that initial binding of katanin p60 KAT1p but not p80 KAT3p is stimulated by glutamylation
-
-
?
ATP + H2O + microtubule
ADP + phosphate + alpha/beta tubulin heterodimers
Tetrahymena thermophila CU428.2
-
katanin-dependent severing of microtubules is important for proper execution of key cellular activities including cell division, migration, and differentiation
-
-
?
ATP + H2O + microtubule
ADP + phosphate + alpha/beta tubulin heterodimers
Tetrahymena thermophila CU428.2
-
activity of katanin requires specific domains of both p60 KAT1p catalytic subunit and p80 KAT3p regulatory subunit. In addition to its activating role, p80 can also contribute to the inhibition of p60 KAT1p. Increased levels of tubulin polyglutamylation correlates with a relocalization of p60 KAT1p to glutamylated microtubules, suggesting that binding of katanin subunits to microtubules is regulated differently and that initial binding of katanin p60 KAT1p but not p80 KAT3p is stimulated by glutamylation
-
-
?
ATP + H2O + microtubule
ADP + phosphate + alpha/beta tubulin heterodimers
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
additional information
?
-
-
direct role of microtubule severing in translocation of the meiotic spindle to the cortex
-
-
?
additional information
?
-
-
the enzyme has multiple effects on microtubules in vitro. Purified MEI-1/MEI-2 complexes preferentially sever at intersections between two microtubules and directly bundle microtubules in vitro. These activities promote parallel/antiparallel microtubule organization in meiotic spindles, MEI-1/MEI-2 complexes bundle microtubules and preferentially sever at intersections between two microtubules in vitro
-
-
?
additional information
?
-
-
enzyme acts on defects in microtubule lattice, promotes loss of tubulin at the defect site until the two microtubule segments are held together so weakly that mechanically unconstrained microtubules kink at the defect site
-
-
?
additional information
?
-
-
enzyme activity regulates the number of microtubule end in mitotic spindle, enzyme inhibition slows the rate of spindle microtubule disassembly
-
-
?
additional information
?
-
katanin p60 destabilizes microtubules at the central spindle and the midbody
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O + microtubule
ADP + phosphate + alpha/beta tubulin heterodimers
assembly of female meiotic spindles requires MEI-1 and MEI-2, which constitute the microtubule-severing AAA+ ATPase Katanin
-
-
?
ATP + H2O + microtubule
ADP + phosphate + alpha/beta tubulin heterodimers
-
-
-
?
ATP + H2O + microtubule
ADP + phosphate + alpha/beta tubulin heterodimers
the enzyme plays important roles in various cellular events including axon regeneration, cytokinesis, and nuclear envelope sealing after mitosis
-
-
?
ATP + H2O + microtubule
ADP + phosphate + alpha/beta tubulin heterodimers
-
katanin-dependent severing of microtubules is important for proper execution of key cellular activities including cell division, migration, and differentiation
-
-
?
ATP + H2O + microtubule
ADP + phosphate + alpha/beta tubulin heterodimers
Tetrahymena thermophila CU428.2
-
katanin-dependent severing of microtubules is important for proper execution of key cellular activities including cell division, migration, and differentiation
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
-
?
additional information
?
-
-
direct role of microtubule severing in translocation of the meiotic spindle to the cortex
-
-
?
additional information
?
-
-
enzyme acts on defects in microtubule lattice, promotes loss of tubulin at the defect site until the two microtubule segments are held together so weakly that mechanically unconstrained microtubules kink at the defect site
-
-
?
additional information
?
-
-
enzyme activity regulates the number of microtubule end in mitotic spindle, enzyme inhibition slows the rate of spindle microtubule disassembly
-
-
?
additional information
?
-
katanin p60 destabilizes microtubules at the central spindle and the midbody
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-[[3-(methylsulfanyl)phenyl]amino]-4-[4-(trifluoromethyl)phenyl]-1H-pyrrole-2,5-dione
-
inhibits microtubule-stimulated ATP hydrolysis by KSP
p80 KAT3p
-
dual character of p80 KAT3p as both an activator and a repressor of p60 KAT1p
-
protein tau
-
affords protection of microtubules in katanin-overexpressing neurons
sb26
-
mutation in the tbb-2 beta-tubulin gene that partially inhibits MEI-1/MEI-2 activity
-
spastin
the basal ATPase activity of spastin is negatively regulated by spastin concentration
-
spg4atg1
morpholino antisense oligonucleotide for blocking translation of spg4 mRNA
-
spg4exon7
morpholino antisense oligonucleotide for blocking correct splicing of spg4 mRNA
-
Tau
-
affords some protection of microtubules in spastin-overexpressing neurons
-
tubulin
tubulin can inhibit severing activity by interfering with katanin binding to microtubules. The inhibition is mediated by the sequence of the tubulin and specifically depends on the carboxy-terminal tails. beta-Tubulin tails are the most effective at inhibiting severing, and detyrosinated alpha-tubulin tails are the least effective
-
additional information
in solution, wild-type katanin is in an autoinhibited state in the presence or absence of nucleotide
-
additional information
-
P-loop substituted mutant of katanin, K-A p60, is a dominant inhibitor of enzyme activity
-
additional information
in solution, wild-type katanin is in an autoinhibited state in the presence or absence of nucleotide
-
additional information
-
dramatically plunge of P60-katanin levels in adult; slightly decline of spastin levels in adult
-
additional information
-
slowed development, shorter axons and fewer axonal branches in spastin-depleted neurons
-
additional information
-
microtubule-severing activity of purified enzyme is inhibited by interphase Xenopus extracts, due to at least 4 separable components, inhibition is reversed by cyclinB/cdk1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-[[3-(methylsulfanyl)phenyl]amino]-4-[4-(trifluoromethyl)phenyl]-1H-pyrrole-2,5-dione
-
accelerates KSP-catalyzed ATP hydrolysis in the absence of microtubules circa 10fold
microtubules
-
SPAS-1's ATPase activity increases with increasing concentrations of microtubules up to 0.00025 mM and then declines at higher microtubule concentrations. In the presence of 0.00025 mM microtubules, ATPase activity is 7times higher than in the absence of microtubules
-
p80 KAT3p
-
dual character of p80 KAT3p as both an activator and a repressor of p60 KAT1p
-
Protein kinase C
-
adseverin upregulation is linked to the chondrocyte maturation program and is regulated by PKC
-
tubulin
at 0.001 mM, up to 6fold stimulation of ATPase activity
-
additional information
-
overexpression of katanin results in 12% loss of microtubule mass, low degradation of microtubule array in katanin-overexpressing neurons
-
additional information
-
overexpression of spastin result in 30% loss of microtubule mass, increase in axonal branching in spastin-overexpressing neurons, degrade of microtubule array in spastin-overexpressing neurons
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.16
ATP
-
DELTA1-226, basal turnover, pH 6.8, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.78
ATP
-
DELTA1-226, basal turnover, pH 6.8, temperature not specified in the publication
3.83
ATP
-
DELTA1-226, microtuble activated turnover, pH 6.8, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0012 - 0.006
3-[[3-(methylsulfanyl)phenyl]amino]-4-[4-(trifluoromethyl)phenyl]-1H-pyrrole-2,5-dione
0.0012
3-[[3-(methylsulfanyl)phenyl]amino]-4-[4-(trifluoromethyl)phenyl]-1H-pyrrole-2,5-dione
-
inhibition of the microtubule-stimulated ATP activity of the ispinesib resistant mutant KHC-L5
0.006
3-[[3-(methylsulfanyl)phenyl]amino]-4-[4-(trifluoromethyl)phenyl]-1H-pyrrole-2,5-dione
-
inhibition of the microtubule-stimulated ATP activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
1-[3'-fluoro-4'-(trifluoromethyl)biphenyl-4-yl]methanamine
Homo sapiens
-
value above 0.02 mM
additional information
3'-fluoro-N,N-dimethyl-4'-(trifluoromethyl)biphenyl-4-sulfonamide
Homo sapiens
-
value above 0.02 mM
additional information
4'-(ethylsulfonyl)-3-fluoro-4-(trifluoromethyl)biphenyl
Homo sapiens
-
value above 0.02 mM
additional information
methyl 3'-fluoro-4'-(trifluoromethyl)biphenyl-4-carboxylate
Homo sapiens
-
value above 0.02 mM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
sea urchin
-
-
brenda
-
-
-
brenda
katanin p60 ATPase-containing subunit A1; gene Katna1
SwissProt
brenda
P60 katanin, enzyme expression changes during development of the nervous system and correlates with axonal growth
SwissProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
lower levels of spastin expression compared with neuronal tissues
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
mostly in the soluble fraction after ultracentrifugation
-
brenda
additional information
-
Dm-Kat60 concentrates at the cell cortex of S2 Drosophila cells during interphase, where it suppresses the polymerization of microtubule plus-ends
brenda
katanin p60 is bundled with microtubules by contractility of the contractile ring and distributed in a microtubule-dependent manner. Katanin p60 localization is restricted in the area of non-growing microtubules during cytokinesis
brenda
-
p60 KAT1p localizes near the basal bodies and in cilia, but also co-localizes with the microtubules of the contractile vacuole. Increased levels of tubulin polyglutamylation correlates with a relocalization of p60 KAT1p to glutamylated microtubules
brenda
Tetrahymena thermophila CU428.2
-
p60 KAT1p localizes near the basal bodies and in cilia, but also co-localizes with the microtubules of the contractile vacuole. Increased levels of tubulin polyglutamylation correlates with a relocalization of p60 KAT1p to glutamylated microtubules
-
brenda
additional information
-
Dm-Kat60 also generally co-localizes with cortical actin. Cortical localization od Dm-Kat60 occurs indepently of microtubules, as it persists following microtubule depolymerization with colchicine
-
brenda
additional information
-
Dm-Kat60 also localizes at the leading edge of migratory D17 Drosophila cells and negatively regulates multiple parameters of their motility
-
brenda
additional information
katanin p60 is localized to both the spindle pole and midbody during mitosis. Localized at the midzone to midbody from anaphase to cytokinesis, the enzyme shows a ring-shaped distribution in the gap between the inside of the contractile ring and the central spindle bundle in telophase. Katanin p60 does not bind with p80 at the midzone or midbody, and localization depends on microtubules. Midbody localization of katanin is dependent on central spindle structure, while Katanin p60 localization in the central spindle is not dependent on contractile ring activity
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme is a member of a family of AAA+ ATPases (ATPase associated with various cellular activities)
malfunction
physiological function
malfunction
-
mutations identified as a major cause of a genetic neurodegenerative condition termed hereditary spastic paraplegia
malfunction
-
point mutations or exon deletions in the microtubule-severing ATPase, spastin, are responsible for approximately 40% of cases of autosomal dominant hereditary spastic paraplegia
malfunction
inhibition of katanin p60 results in incomplete cytokinesis by regression and thus caused the appearance of binucleate cells
malfunction
-
rapid inactivation of katanin results in complete loss of ASPM-1 positive spindle poles. Strong loss-of-function mutants assemble apolar intersecting microtubule arrays, whereas weaker mutants assemble bipolar meiotic spindles that are longer than wild-type. Microtubule disassembly in enzyme point mutants, overview. Progressive loss of katanin leads to a progressive loss in the organization of pole-to-pole microtubule bundles, phenotypes
malfunction
cells overexpressing Kat60 display a disorganized array of fragmented microtubules and the overall length of microtubules appears to decrease with increasing levels of Kat60. Depletion of catalytic subunit Kat60 and regulatory subunit Kat80 causes minimal perturbation of steady-state alpha-tubulin levels in cells
malfunction
KATANIN 1 mutants, fra2, lue1 and ktn1-2 collectively display lower fertility and seed set in Arabidopsis. The lower fertility and seed set rates of fra2, lue1 and ktn1-2 mutants are correlated to abnormalities in the development of embryo proper and seed
malfunction
variants show disorganized microtubules that lack focused spindle poles reminiscent of the Katanin loss-of-function phenotype, demonstrating that the microtubule-severing activity is essential for meiotic spindle assembly in Caenorhabditis elegans
malfunction
-
KATANIN 1 mutants, fra2, lue1 and ktn1-2 collectively display lower fertility and seed set in Arabidopsis. The lower fertility and seed set rates of fra2, lue1 and ktn1-2 mutants are correlated to abnormalities in the development of embryo proper and seed
-
physiological function
-
katanin p60, a microtubule-severing enzyme plays a key role in cytoskeletal reorganization during various cellular events in an ATP-dependent manner
physiological function
-
SPAS-1 shows microtubule-severing activity when expresses in cultured cells. When alpha/beta tubulin dimer is incubated with SPAS-1, tubulin is pulled down with SPAS-1, suggesting the Caenorhabditis elegans SPAS-1 binds to tubulin
physiological function
functional experiments indicate that spastin depletion results in reduced cell motility and higher cell proliferation of glioblastoma cell line T98G cells
physiological function
katanin is a microtubule-severing protein comprised of an AAA+ ATPase subunit and an accessory subunit designated as p60 and p80, respectively. Katanin p60 (ATPase-containing) subunit A1 does not bind with p80 at the midzone or midbody, and localization depends on microtubules. At the central spindle and the midbody, no microtubule growth plus termini are seen with katanin p60, and microtubule density is inversely correlated with katanin p60 density in the region of katanin p60 localization that seems to lead to microtubule destabilization at the midbody. Katanin p60 contributes to microtubule instability at the midzone and midbody and facilitates cytokinesis in rat cells, microtubule destabilization function of katanin p60 at the midzone and the midbody during cell division contributing to accurate cytokinesis
physiological function
-
katanin maintains meiotic metaphase chromosome alignment and spindle structure in vivo. Assembly of Caenorhabditis elegans female meiotic spindles requires both MEI-1 and MEI-2 subunits of the microtubule-severing ATPase katanin. A linear relationship between in vitro microtubule disassembly rates and in vivo spindle length exists
physiological function
assembly of female meiotic spindles requires MEI-1 and MEI-2, which constitute the microtubule-severing AAA+ ATPase Katanin
physiological function
Katanin A subunit catalyzes the microtubule-severing activity during mitosis. It likely coordinates with KATNB1 to perform this function. KATNBL1 is a regulator of mammalian Katanin microtubule-severing
physiological function
-
katanin is a negative regulator of microtubule minus-end stabilization by CAMSAPs proteins
physiological function
-
katanin-dependent severing of microtubules is important for proper execution of key cellular activities including cell division, migration, and differentiation
physiological function
reduction in KATANIN expression inhibits formation of adventitious roots and indirectly influences the specific expression of some microtubule-associated proteins
physiological function
the enzyme fulfills a major regulatory mechanism of dynamic microtubule turnover in eukaryotes. It is essential for embryogenesis and seed formation in Arabidopsis
physiological function
the enzyme plays important roles in various cellular events including axon regeneration, cytokinesis, and nuclear envelope sealing after mitosis
physiological function
Tetrahymena thermophila CU428.2
-
katanin-dependent severing of microtubules is important for proper execution of key cellular activities including cell division, migration, and differentiation
-
physiological function
-
the enzyme fulfills a major regulatory mechanism of dynamic microtubule turnover in eukaryotes. It is essential for embryogenesis and seed formation in Arabidopsis
-
physiological function
-
reduction in KATANIN expression inhibits formation of adventitious roots and indirectly influences the specific expression of some microtubule-associated proteins
-
Show AA Sequence and Transmembrane Helices (4640 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
350000
-
hexamer, GST-free spastin, determined by gel filtration analysis and Western blotting
50000
52000
530000
-
hexamer, GST-spastin, determined by gel filtration analysis and Western blotting
54400
55000
57000
-
SPAS-1L, consists of nine exons, determined by SDS-PAGE and Western blotting
58000
60000
62000
62200
spastin isoform: 1st ATG, predicted molecular weight of the isoform tagged with His6
63600
80000
81000
88000
-
monomer, GST-spastin, determined by gel filtration analysis and Western blotting
50000
-
SPAS-1S, consists of eight exons, determined by SDS-PAGE and Western blotting
52000
-
1 * 52000, SDS-PAGE, when low concentrations of SPAS-1 (below 0.55 mg/ml) are analyzed, stable hexamers are not formed, rather it shows a broad elution profile over monomer to hexamer, even in the presence of ATP
54400
spastin isoform: splice variant lacking exon 4, 2nd ATG, predicted molecular weight of the isoform tagged with His6
55000
-
Western analysis using a polyclonal antibody against the 60 kDa subunit of human katanin
58000
spastin isoform: 2nd ATG, predicted molecular weight of the isoform tagged with His6
60000
-
1 * 80000 + 1 * 60000, SDS-PAGE
63600
spastin isoform: splice variant lacking exon 4, 1st ATG, predicted molecular weight of the isoform tagged with His6
80000
-
1 * 80000 + 1 * 60000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterodimer
heterotetramer
hexamer
homohexamer
monomer
additional information
?
Q9WV86; Q8BG40
the enzyme consists two subunits, the catalytic p60 subunit and the p80 subunit. ADP-bound p60 is typically monomeric and exchange of ADP to ATP induces hexamerization. The hexameric p60 subunit is active alone, its association with the p80 subunit greatly enhances both the microtubule-binding and microtubule-severing activities of katanin. The interaction between the two katanin subunits is mediated by the p60-MIT domain and the p80 C-terminal domain
dimer
-
1 * 80000 + 1 * 60000, SDS-PAGE
heterodimer
katanin is a heterodimer composed of a catalytic subunit that hydrolyses ATP to sever microtubules, and a regulatory subunit involved in subcellular targeting
heterodimer
-
catalytic and non-catalytic domain together form hexameric rings
heterodimer
-
MEI-1 and MEI-2 are the Caenorhabditis elegans homologs of the p60 (catalytic) and the p80 (localization) subunits
heterodimer
-
P60-katanin severs microtubules, P80-katanin targets a portion of the katanin to the centrosome
heterodimer
-
composed of an AAA domain catalytic subunit, p60, and a regulatory subunit, a WD40 repeat protein, p80
heterodimer
Tetrahymena thermophila CU428.2
-
composed of an AAA domain catalytic subunit, p60, and a regulatory subunit, a WD40 repeat protein, p80
-
heterotetramer
heterotetramer of KATNAL1/B1 (an ATPase associated with diverse cellular activities) and the regulatory subunit con80. It does not assemble beyond a dimer of heterodimers (heterotetramer), even at concentrations up to 0.05 mM
heterotetramer
heterotetramer of KATNAL1/B1 (an ATPase associated with diverse cellular activities) and the regulatory subunit con80. It does not assemble beyond a dimer of heterodimers (heterotetramer), even at concentrations up to 0.05 mM
hexamer
-
SPAS-1 forms a stable hexamer in a concentration-dependent manner. The microtubule binding domain MTBD of SPAS-1 plays a critical role in enrichment of SPAS-1 to microtubules, where SPAS-1 is concentrated above 5 mg/ml and able to form a stable hexamer. Hexamer formation takes place in an ATP-independent manner
hexamer
MEI-2 subunit stabilizes the MEI-1 hexamer for optimal ATP-dependent microtubule severing
hexamer
-
full length protein, hexameric ring, sedimentation velocity and gel filtration assays
monomer
-
Arabidopsis thaliana katanin small subunit, AtKSS, is the p60 homolog in plants, a putative p80 homolog is decribed elsewhere
monomer
-
1 * 52000, SDS-PAGE, when low concentrations of SPAS-1 (below 0.55 mg/ml) are analyzed, stable hexamers are not formed, rather it shows a broad elution profile over monomer to hexamer, even in the presence of ATP
additional information
data suggest that AtKSS oligomerizes into a ring-shaped oligomer, and that the microtubule-binding domain is involved in the oligomerization process, the addition of two trimers to form a hexamer is proposed
additional information
-
data suggest that AtKSS oligomerizes into a ring-shaped oligomer, and that the microtubule-binding domain is involved in the oligomerization process, the addition of two trimers to form a hexamer is proposed
additional information
-
a single domain isolated from the N-terminus of mouse katanin P60 binds to tubulin
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop method at 20°C, crystal structure of MEI-1 AAA ATPase in the ADP-bound state reveals a pseudo-hexameric left-handed spiral assembly
secondary structure analyzed by circular dichroism (CD) spectrum. SPAS-1 retains a high degree of alpha-helical structure
-
the X-ray structure of the nucleotide-free, monomeric AAA domain of Drosophila melanogaster spastin, residues 464-758, is solved at a resolution of 2.7 A
hanging drop method, the N-terminal residues (about 10000 Da) are clipped off during time of crystal formation (5-7 days)
-
hanging-drop method at 20°C, crystal structure of KATNAL1 AAA ATPase in the nucleotide-free state reveals a monomer
high-resolution structure of the heterodimeric complex of p60-microtubule interacting and trafficking domain and the p80 C-terminal domain is determined by X-ray crystallography
Q9WV86; Q8BG40
the structure of kp60-NTD reveals a striking similarity to those of the microtubule interacting and trafficking domains (MIT). The arragnement of helices 2 and 3 is well conserved between kp60-NTD and the MIT domain from Vps4, a homologous protein that promotes disassembly of the endosomal sorting complexes required for transport III membrane skeleton complex. The positively charged surface formed by helices 2 and 3 binds tubulin
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K437P/K441P
predicted not to form the C-terminal alpha-helix, microtuble network remains in mutant protein expressing HEK293 cells
1-279STOP
-
deletion mutant, no severing of microtubules, no binding of microtubules
1-328STOP
-
deletion mutant, no severing of microtubules, but binding of microtubules
DELTAMTBD
-
deletion mutant lacking aa 1-227 and 270-328, neither binds nor severs microtubules
E356A
the basal ATPase activity is severely compromised to undetectable levels
E442Q
fragment 227-279
-
fragment consisting of aa 227-279, no severing of microtubules, no binding of microtubules
fragment 227-328
-
fragment consisting of aa 227-328, no severing of microtubules, but binding of microtubules
K388R
P45Q
leading to an early onset severe form of hereditary spastic paraplegia when present in heterozygosity with a mutant allele
R499C
R562Q
the basal ATPase activity is severely compromised to undetectable levels
S44L
leading to an early onset severe form of hereditary spastic paraplegia when present in heterozygosity with a mutant allele
K255A
A323V
-
mutant dgl1-1, exhibits different response to gibberellin and/or brassinosteroid
D483N
-
mutant dgl1-2, exhibits different response to gibberellin and/or brassinosteroid
DELTA241-408
-
mutant dgl1-3, exhibits different response to gibberellin and/or brassinosteroid
additional information
E442Q
-
mutant harboring a canonical Walker B motif point mutation, predicted to bind but not hydrolyze ATP
E442Q
-
residue of Walker B motif, hydrolysis deficient mutant, amino acid residues 228-616
E442Q
neutralization of the positive charges in the microtubule-binding domain (MTBD) of spastin, resulting in the spastin-allA mutant, dramatically decreases the ATPase activity at low concentration, although the ATP-hydrolyzing potential is not affected. The ATP-hydrolyzing activity of spastin-allA is stimulated to varying levels by the ATPase-deficient E442Q mutant, depending on whether the microtubule-binding domain is intact
K255A
-
mutant, dominant inhibitor of mouse p60, fused with RFP driven by CMV promoter
additional information
-
homozygotic gene disruption mutants, meiotic spindles move to the cortex, but association with cortex is unstable
additional information
-
mei-1(null): mutant lacking katanin activity, mei-1(gf): gain-of-function mutant
additional information
-
mutational analysis reveals that the conserved exposed, basic amino acid residues in the pore region of stastin as well as the aromatic residue are important for the recognition and severing of microtubules. The conformational change of W251 is detected upon ATP binding by measuring the fluorescence emission spectra of tryptophan. Given that K257 is located close to the corresponding aromatic residue W251, it seems possible that K257 is also involved in a mechanochemical process from conformational change of W251 in microtubule severing
additional information
C-terminal deletion mutants: 1-432, 1-435, 1-447, C-terminal alpha-helix is essential for microtuble severing
additional information
-
C-terminal deletion mutants: 1-432, 1-435, 1-447, C-terminal alpha-helix is essential for microtuble severing
additional information
-
deltaTM D-spastin-GFP: construct lacking the transmembrane-containing N-terminus, diffusely distributed in the cytoplasm, fully active for disassembling cytoplasmatic microtubules. TM+MIT: construct lacking the AAA domain, do not affect the microtubule cytoskeleton. MIT: MIT domain alone, diffusely distributed and do not disassemble microtubules. AAA: AAA domain alone, diffusely distributed and do not disassemble microtubules.
additional information
expression of a dominant-negative enzyme construct inhibits microtubule severing and is deleterious to axonal growth. Overexpression of wild-type enzyme results in excess microtubule severing and is also deleterious to axonal growth in some of the neurons
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
47
-
the melting temperature Tm is estimated from the denaturation curve
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
GSH-Sepharose affinity chromatography, ion exchange chromatography, cleavage with precission protease, GSH-Sepharose affinity chromatography and gel filtration
-
GSTrap column chromatography, GST tag cleaved with PreScission Protease, GST-Sepharose chromatography, gel filtration
-
purification of recombinant protein using a glutathione-sepharose column, removing of the GST moiety with precision protease
-
recombinant glutathione S-transferase-tagged form kp60-NTD, affinity purification on glutathione-Sepharose and dialysis
-
recombinant His-tagged katanin p60 subunit from Escherichia coli strain BL21(DE3) pLysS by nickel affinity chromatography to over 95% purity
recombinant untagged short isoform of MEI-1 subunit and MBP-TEV-tagged MEI-2 subunit from Escherichia coli by amylose affinity chromatography, eluted with TEV protease
-
using a glutathione-agarose column, the glutathione-S-transferase moiety is cleaved with thrombin
-
using a glutathione-Sepharose column, cleavage of the GST moiety with PreScission Protease
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a glutathione S-transferase-tagged form of kp60-NTD expressed in Escherichia coli BL21 (DE3)
-
adaptor-p80 fragments expressed in Escherichia coli BL21(DE3), GST tagged p60-katanin expressed in Escherichia coli JM109
baculo system for pull-down assay, TNT in vitro translation kit for S35-Met-labeled recombinant protein, cloned into pEGFP or pcDNA3.1 for transfection of COS-7 cells for immuno precipitation
-
cDNA in TA cloning vector for sequencing, for expression in cultured neurons or fibroblasts in pEGFP and pCMV-Tag vector
-
cloning of Cp60 katanin cDNA, expressed in Escherichia coli BL21(DE3)
-
expressed in Escherichia coli BL21(DE3), FLAG tagged versions expressed in HEK293 cells
expression of the selenomethionine-substituted (Se-MEI-1/MEI-2) katanin complex in Escherichia coli BL21
gene Katna1, cloning of the enzyme katanin p60 subunit from rat liver, recombinant expression of His-tagged protein in Escherichia coli strain BL21(DE3) pLysS
GST fusion of amino acid residues 228-616 containing the E442Q mutation (42500 Da for the 389 amino acid residues construct (amino acid residues 228-616)), expressed in Escherichia coli BL21-CodonPlus (DE3)-RIPL
-
human spastin was cloned into the pGBK-T7 plasmid for yeast two-hybrid screening
-
into pQE30 vector, His-tag, and pGEX 4T3, GST-fusion, for expression in Escherichia coli
into the pGEX-6P-3 vector for expression in Escherichia coli BL21-CodonPlus DE3-RIPL cells
-
isolation of cDNA clones for the p60 and p80 subunits, heterologous expression of p60 in Sf9 cell baculovirus system
-
mouse p80-CTD (residues 481-658) are cloned into a modified version of the pET-15b vector, pHisTrx2, which includes Escherichia coli thioredoxin A as a fusion protein after the His6 tag
Q9WV86; Q8BG40
overexpression of the catalytic subunit Kat60 in Drosophila S2 cells
pBSK vector for subcloning of the PCR products, pACN and pbinSRN for generating plasmids coding for fusion constructs of the target protein
-
recombinant expression of untagged short isoform of MEI-1 subunit, coexpression with MBP-TEV-tagged MEI-2 subunit, in Escherichia coli
-
SPAS-1 protein (451 amino acid reisdues) is produced as an N-terminally His6-tagged recombinant protein, expressed in Escherichia coli BL21(DE3)
-
spastin cDNA is cloned into the pGEMT easy vector, for generating a bait construct for yeast two-hybrid analysis, the excised spastin fragment is cloned into the pGBKT7 vector, for expression analysis in mammalian cells, the fragment is cloned into the pCS2-myc and pEGFP-C1 vectors
-
spastin cDNA was cloned into pGEX6p-3 for production of recombinant protein in Escherichia coli or into pEYFP-C1
-
TA-cloned for sequencing, subcloned into pFLAG-CMV-6a for transfection of HEK293 cells
the human short isoform of spastin initiating from the alternative start codon is amplified by PCR and cloned into the pET41a vector for expression in Escherichia coli BL21DE3 cells
-
the motor domain of wild-type KSP monomer, aa 1-360, is expressed in Escherichia coli BL21DE3 cells
-
three domains of AtKSS are defined, AtKSS1, aa 1-34, AtKSS2, aa 35-210, AtKSS3, the ATPase domain, aa 211-523, in addition, combinations are defined, AtKKS12 and AtKKS23, AtKSS1,2,3,12,and 23 are cloned into pGEX-4T-1 and pOL-LT plasmids
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cells induced to express the catalytic subunit Kat60 have reduced levels of alpha-tubulin compared to control cells
expression and cellular distribution are increased in neoplastic glial phenotypes, especially in glioblastoma
overexpression of both, p80 KAT3p and p60 KAT1p enhances the rate of disassembly of microtubular structures as compared with overexpression of p60 KAT1p alone
reduction in KATANIN expression inhibits formation of adventitious roots and indirectly influences the specific expression of some microtubule-associated proteins
overexpression of both, p80 KAT3p and p60 KAT1p enhances the rate of disassembly of microtubular structures as compared with overexpression of p60 KAT1p alone
-
overexpression of both, p80 KAT3p and p60 KAT1p enhances the rate of disassembly of microtubular structures as compared with overexpression of p60 KAT1p alone
Tetrahymena thermophila CU428.2
-
-
reduction in KATANIN expression inhibits formation of adventitious roots and indirectly influences the specific expression of some microtubule-associated proteins
reduction in KATANIN expression inhibits formation of adventitious roots and indirectly influences the specific expression of some microtubule-associated proteins
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
a major fraction of autosomal dominant cases of hereditary spastic paraplegia (HSP) is caused by mutations in SPG4 encoding spastin
medicine
-
hereditary spastic paraplegias (HSPs) are most commonly caused by mutations in the spastin gene
medicine
-
mutations cause an autosomal dominant form of hereditary spastic paraplegia
medicine
mutations in the SPG4 gene, spastin is the SPG4 gene product, are the most common cause of autosomal dominant hereditary spastic paraplegia, HSP
medicine
the most frequently mutated gene causing autosomal dominant hereditary spastic paraplegias is SPG4, which encodes spastin
medicine
-
spastin is mutated in the neurodegenerative disease hereditary spastic paraplegia
medicine
-
spastin is the most commonly mutated protein in hereditary spastic paraplegia
medicine
spg4, the gene encoding for spastin, is mutated in around 40% of cases of autosomal dominant hereditary spastic paraplegia
medicine
the analysis provides insights into the structural defects in spastin that arise from mutations identified in hereditary paraplegia patients
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
McNally, F.J.; Vale, R.D.
Identification of katanin, an ATPase that severs and disassembles stable microtubules
Cell
75
419-429
1993
Actinocoryne sp., Chlamydomonas reinhardtii, Spisula solidissima, Strongylocentrotus purpuratus, Xenopus laevis
brenda
McNally, F.J.; Okawa, K.; Iwamatsu, A.; Vale, R.D.
Katanin, the microtubule-severing ATPase, is concentrated at centrosomes
J. Cell Sci.
109
561-567
1996
Strongylocentrotus purpuratus, Xenopus laevis
brenda
Hartman, J.J.; Mahr, J.; McNally, K.; Okawa, K.; Iwamatsu, A.; Thomas, S.; Cheesman, S.; Heuser, J.; Vale, R.D.; McNally, F.J.
Katanin, a microtubule-severing protein, is a novel AAA ATPase that targets to the centrosome using a WD40-containing subunit
Cell
93
277-287
1998
Saccharomyces cerevisiae, Caenorhabditis elegans, Dictyostelium sp., Drosophila sp. (in: flies), Homo sapiens, Strongylocentrotus purpuratus, Xenopus laevis
brenda
Lohret, T.A.; McNally, F.J.; Quarmby, L.M.
A role for katanin-mediated axonemal severing during Chlamydomonas deflagellation
Mol. Biol.
9
1195-1207
1998
Chlamydomonas reinhardtii, Homo sapiens, Strongylocentrotus purpuratus, Xenopus laevis
brenda
McNally, F.J.; Thomas, S.
Katanin is responsible for the M-phase microtubule-severing activity in Xenopus eggs
Mol. Biol.
9
1847-1861
1998
Caenorhabditis elegans, Gallus gallus, Chlamydomonas reinhardtii, Mus musculus, Strongylocentrotus purpuratus, Xenopus laevis, Homo sapiens (O75449), Homo sapiens
brenda
Lohret, T.A.; Zhao, L.; Quarmby, L.M.
Cloning of Chlamydomonas p60 katanin and localization to the site of outer doublet severing during deflagellation
Cell Motil. Cytoskeleton
43
221-231
1999
Chlamydomonas reinhardtii, Homo sapiens, Strongylocentrotus purpuratus, Xenopus laevis
brenda
Ahmad, F.J.; Yu, W.; McNally, F.J.; Baas, P.W.
An essential role for katanin in severing microtubules in the neuron
J. Cell Biol.
145
305-315
1999
Homo sapiens, Rattus norvegicus, Strongylocentrotus purpuratus
brenda
Quarmby, L.
Cellular Samurai: katanin and the severing of microtubules
J. Cell Sci.
113
2821-2827
2000
Arabidopsis sp., Caenorhabditis elegans, Chlamydomonas reinhardtii, Drosophila sp. (in: flies), Homo sapiens, no activity in Saccharomyces cerevisiae, Xenopus laevis
brenda
Stoppin-Mellet, V.; Gaillard, J.; Vantard, M.
Functional evidence for in vitro microtubule severing by the plant katanin homologue
Biochem. J.
365
337-342
2002
Arabidopsis thaliana (Q9SEX2), Arabidopsis thaliana
brenda
Davis, L.J.; Odde, D.J.; Block, S.M.; Gross, S.P.
The importance of lattice defects in katanin-mediated microtubule severing in vitro
Biophys. J.
82
2916-2927
2002
Echinoidea
brenda
McNally, K.P.; Buster, D.; McNally, F.J.
Katanin-mediated microtubule severing can be regulated by multiple mechanisms
Cell Motil. Cytoskeleton
53
337-349
2002
Xenopus laevis
brenda
Yang, H.Y.; McNally, K.; McNally, F.J.
MEI-1/katanin is required for translocation of the meiosis I spindle to the oocyte cortex in C. elegans
Dev. Biol.
260
245-259
2003
Caenorhabditis elegans
brenda
Dymek, E.E.; Lefebvre, P.A.; Smith, E.F.
PF15p is the Chlamydomonas homologue of the katanin p80 subunit and is required for assembly of flagellar central microtubules
Eukaryot. Cell
3
870-879
2004
Chlamydomonas reinhardtii (Q6PLH8)
brenda
Buster, D.; McNally, K.; McNally, F.J.
Katanin inhibition prevents the redistribution of gamma-tubulin at mitosis
J. Cell Sci.
115
1083-1092
2002
Homo sapiens
brenda
Karabay, A.; Yu, W.; Solowska, J.M.; Baird, D.H.; Baas, P.W.
Axonal growth is sensitive to the levels of katanin, a protein that severs microtubules
J. Neurosci.
24
5778-5788
2004
Rattus norvegicus (Q6E0V2)
brenda
Roll-Mecak, A.; Vale, R.D.
The Drosophila homologue of the hereditary spastic paraplegia protein, spastin, severs and disassembles microtubules
Curr. Biol.
15
650-655
2005
Drosophila melanogaster
brenda
Srayko, M.; Otoole, E.T.; Hyman, A.A.; Mueller-Reichert, T.
Katanin disrupts the microtubule lattice and increases polymer number in C. elegans meiosis
Curr. Biol.
16
1944-1949
2006
Caenorhabditis elegans
brenda
Ribbeck, K.; Mitchison, T.J.
Meiotic spindle: sculpted by severing
Curr. Biol.
16
R923-R925
2006
Caenorhabditis elegans
brenda
Nurminsky, D.; Magee, C.; Faverman, L.; Nurminskaya, M.
Regulation of chondrocyte differentiation by actin-severing protein adseverin
Dev. Biol.
302
427-437
2007
Gallus gallus
brenda
Toyo-Oka, K.; Sasaki, S.; Yano, Y.; Mori, D.; Kobayashi, T.; Toyoshima, Y.Y.; Tokuoka, S.M.; Ishii, S.; Shimizu, T.; Muramatsu, M.; Hiraiwa, N.; Yoshiki, A.; Wynshaw-Boris, A.; Hirotsune, S.
Recruitment of katanin p60 by phosphorylated NDEL1, an LIS1 interacting protein, is essential for mitotic cell division and neuronal migration
Hum. Mol. Genet.
14
3113-3128
2005
Mus musculus
brenda
Wood, J.D.; Landers, J.A.; Bingley, M.; McDermott, C.J.; Thomas-McArthur, V.; Gleadall, L.J.; Shaw, P.J.; Cunliffe, V.T.
The microtubule-severing protein Spastin is essential for axon outgrowth in the zebrafish embryo
Hum. Mol. Genet.
15
2763-2771
2006
Danio rerio (Q6NW58), Danio rerio
brenda
Evans, K.J.; Gomes, E.R.; Reisenweber, S.M.; Gundersen, G.G.; Lauring, B.P.
Linking axonal degeneration to microtubule remodeling by Spastin-mediated microtubule severing
J. Cell Biol.
168
599-606
2005
Homo sapiens
brenda
Salinas, S.; Carazo-Salas, R.E.; Proukakis, C.; Cooper, J.M.; Weston, A.E.; Schiavo, G.; Warner, T.T.
Human spastin has multiple microtubule-related functions
J. Neurochem.
95
1411-1420
2005
Homo sapiens (Q9UBP0), Homo sapiens
brenda
Yu, W.; Solowska, J.M.; Qiang, L.; Karabay, A.; Baird, D.; Baas, P.W.
Regulation of microtubule severing by katanin subunits during neuronal development
J. Neurosci.
25
5573-5583
2005
Rattus norvegicus
brenda
Qiang, L.; Yu, W.; Andreadis, A.; Luo, M.; Baas, P.W.
Tau protects microtubules in the axon from severing by katanin
J. Neurosci.
26
3120-3129
2006
Rattus norvegicus
brenda
Lu, C.; Srayko, M.; Mains, P.E.
The Caenorhabditis elegans microtubule-severing complex MEI-1/MEI-2 katanin interacts differently with two superficially redundant beta-tubulin isotypes
Mol. Biol. Cell
15
142-150
2004
Caenorhabditis elegans
brenda
Schickel, J.; Beetz, C.; Froemmel, C.; Heide, G.; Sasse, A.; Hemmerich, P.; Deufel, T.
Unexpected pathogenic mechanism of a novel mutation in the coding sequence of SPG4 (spastin)
Neurology
66
421-423
2006
Homo sapiens
brenda
Stoppin-Mellet, V.; Gaillard, J.; Vantard, M.
Katanins severing activity favors bundling of cortical microtubules in plants
Plant J.
46
1009-1017
2006
Arabidopsis thaliana
brenda
Komorisono, M.; Ueguchi-Tanaka, M.; Aichi, I.; Hasegawa, Y.; Ashikari, M.; Kitano, H.; Matsuoka, M.; Sazuka, T.
Analysis of the rice mutant dwarf and gladius leaf 1. Aberrant katanin-mediated microtubule organization causes up-regulation of gibberellin biosynthetic genes independently of gibberellin signaling
Plant Physiol.
138
1982-1993
2005
Oryza sativa
brenda
Evans, K.; Keller, C.; Pavur, K.; Glasgow, K.; Conn, B.; Lauring, B.
Interaction of two hereditary spastic paraplegia gene products, spastin and atlastin, suggests a common pathway for axonal maintenance
Proc. Natl. Acad. Sci. USA
103
10666-10671
2006
Homo sapiens
brenda
Matsushita-Ishiodori, Y.; Yamanaka, K.; Ogura, T.
The C. elegans homologue of the spastic paraplegia protein, spastin, disassembles microtubules
Biochem. Biophys. Res. Commun.
359
157-162
2007
Caenorhabditis elegans
brenda
Luo, L.; Carson, J.D.; Molnar, K.S.; Tuske, S.J.; Coales, S.J.; Hamuro, Y.; Sung, C.M.; Sudakin, V.; Auger, K.R.; Dhanak, D.; Jackson, J.R.; Huang, P.S.; Tummino, P.J.; Copeland, R.A.
Conformation-dependent ligand regulation of ATP hydrolysis by human KSP - activation of basal hydrolysis and inhibition of microtubule-stimulated hydrolysis by a single, small molecule modulator
J. Am. Chem. Soc.
130
7584-7591
2008
Homo sapiens
brenda
White, S.R.; Evans, K.J.; Lary, J.; Cole, J.L.; Lauring, B.
Recognition of C-terminal amino acids in tubulin by pore loops in Spastin is important for microtubule severing
J. Cell Biol.
176
995-1005
2007
Homo sapiens
brenda
Pantakani, D.V.; Swapna, L.S.; Srinivasan, N.; Mannan, A.U.
Spastin oligomerizes into a hexamer and the mutant spastin (E442Q) redistribute the wild-type spastin into filamentous microtubule
J. Neurochem.
106
613-624
2008
Homo sapiens
brenda
Salinas, S.; Carazo-Salas, R.E.; Proukakis, C.; Schiavo, G.; Warner, T.T.
Spastin and microtubules - Functions in health and disease
J. Neurosci. Res.
85
2778-2782
2007
Homo sapiens (Q9UBP0)
brenda
Roll-Mecak, A.; Vale, R.D.
Structural basis of microtubule severing by the hereditary spastic paraplegia protein spastin
Nature
451
363-367
2008
Drosophila melanogaster (Q8I0P1)
brenda
Mannan, A.U.; Boehm, J.; Sauter, S.M.; Rauber, A.; Byrne, P.C.; Neesen, J.; Engel, W.
Spastin, the most commonly mutated protein in hereditary spastic paraplegia interacts with Reticulon 1 an endoplasmic reticulum protein
Neurogenetics
7
93-103
2006
Homo sapiens
brenda
Stoppin-Mellet, V.; Gaillard, J.; Timmers, T.; Neumann, E.; Conway, J.; Vantard, M.
Arabidopsis katanin binds microtubules using a multimeric microtubule-binding domain
Plant Physiol. Biochem.
45
867-877
2007
Arabidopsis thaliana (Q9SEX2), Arabidopsis thaliana
brenda
Matsuno, K.; Sawada, J.; Sugimoto, M.; Ogo, N.; Asai, A.
Bis(hetero)aryl derivatives as unique kinesin spindle protein inhibitors
Bioorg. Med. Chem. Lett.
19
1058-1061
2009
Homo sapiens
brenda
Mancuso, G.; Rugarli, E.I.
A cryptic promoter in the first exon of the SPG4 gene directs the synthesis of the 60-kDa spastin isoform
BMC Biol.
6
31
2008
Homo sapiens (Q9UBP0)
brenda
Solowska, J.M.; Morfini, G.; Falnikar, A.; Himes, B.T.; Brady, S.T.; Huang, D.; Baas, P.W.
Quantitative and functional analyses of spastin in the nervous system: implications for hereditary spastic paraplegia
J. Neurosci.
28
2147-2157
2008
Rattus norvegicus
brenda
Yu, W.; Qiang, L.; Solowska, J.M.; Karabay, A.; Korulu, S.; Baas, P.W.
The microtubule-severing proteins spastin and katanin participate differently in the formation of axonal branches
Mol. Biol. Cell
19
1485-1498
2008
Rattus norvegicus
brenda
Connell, J.W.; Lindon, C.; Luzio, J.P.; Reid, E.
Spastin couples microtubule severing to membrane traffic in completion of cytokinesis and secretion
Traffic
10
42-56
2009
Homo sapiens (Q9UBP0)
brenda
Matsushita-Ishiodori, Y.; Yamanaka, K.; Hashimoto, H.; Esaki, M.; Ogura, T.
Conserved aromatic and basic amino acid residues in the pore region of Caenorhabditis elegans spastin play critical roles in microtubule severing
Genes Cells
14
925-940
2009
Caenorhabditis elegans
brenda
Iwaya, N.; Kuwahara, Y.; Fujiwara, Y.; Goda, N.; Tenno, T.; Akiyama, K.; Mase, S.; Tochio, H.; Ikegami, T.; Shirakawa, M.; Hiroaki, H.
A common substrate recognition mode conserved between katanin p60 and VPS4 governs microtubule severing and membrane skeleton reorganization
J. Biol. Chem.
285
16822-16829
2010
Mus musculus
brenda
Zhang, D.; Grode, K.D.; Stewman, S.F.; Diaz-Valencia, J.D.; Liebling, E.; Rath, U.; Riera, T.; Currie, J.D.; Buster, D.W.; Asenjo, A.B.; Sosa, H.J.; Ross, J.L.; Ma, A.; Rogers, S.L.; Sharp, D.J.
Drosophila katanin is a microtubule depolymerase that regulates cortical-microtubule plus-end interactions and cell migration
Nat. Cell Biol.
13
361-369
2011
Drosophila melanogaster
brenda
Lumb, J.H.; Connell, J.W.; Allison, R.; Reid, E.
The AAA ATPase spastin links microtubule severing to membrane modelling
Biochim. Biophys. Acta
1823
192-197
2012
Homo sapiens
brenda
Iwaya, N.; Akiyama, K.; Goda, N.; Tenno, T.; Fujiwara, Y.; Hamada, D.; Ikura, T.; Shirakawa, M.; Hiroaki, H.
Effect of Ca2+ on the microtubule-severing enzyme p60-katanin. Insight into the substrate-dependent activation mechanism
FEBS J.
279
1339-1352
2012
Mus musculus (Q9WV86)
brenda
Eckert, T.; Link, S.; Le, D.T.; Sobczak, J.P.; Gieseke, A.; Richter, K.; Woehlke, G.
Subunit interactions and cooperativity in the microtubule-severing AAA ATPase spastin
J. Biol. Chem.
287
26278-26290
2012
Homo sapiens
brenda
Draberova, E.; Vinopal, S.; Morfini, G.; Liu, P.S.; Sladkova, V.; Sulimenko, T.; Burns, M.R.; Solowska, J.; Kulandaivel, K.; de Chadarevian, J.P.; Legido, A.; Moerk, S.J.; Janacek, J.; Baas, P.W.; Draber, P.; Katsetos, C.D.
Microtubule-severing ATPase spastin in glioblastoma: increased expression in human glioblastoma cell lines and inverse roles in cell motility and proliferation
J. Neuropathol. Exp. Neurol.
70
811-826
2011
Homo sapiens (Q9UBP0), Homo sapiens
brenda
Taylor, J.; White, S.; Lauring, B.; Kull, F.
Crystal structure of the human spastin AAA domain
J. Struct. Biol.
179
133-137
2012
Homo sapiens
brenda
Onitake, A.; Matsushita-Ishiodori, Y.; Johjima, A.; Esaki, M.; Ogura, T.; Yamanaka, K.
The C-terminal alpha-helix of SPAS-1, a Caenorhabditis elegans spastin homologue, is crucial for microtubule severing
J. Struct. Biol.
179
138-142
2012
Caenorhabditis elegans (Q8MNV0), Caenorhabditis elegans
brenda
McNally, K.; Berg, E.; Cortes, D.B.; Hernandez, V.; Mains, P.E.; McNally, F.J.
Katanin maintains meiotic metaphase chromosome alignment and spindle structure in vivo and has multiple effects on microtubules in vitro
Mol. Biol. Cell
25
1037-1049
2014
Caenorhabditis elegans
brenda
Matsuo, M.; Shimodaira, T.; Kasama, T.; Hata, Y.; Echigo, A.; Okabe, M.; Arai, K.; Makino, Y.; Niwa, S.; Saya, H.; Kishimoto, T.
Katanin p60 contributes to microtubule instability around the midbody and facilitates cytokinesis in rat cells
PLoS ONE
8
e80392
2013
Rattus norvegicus (Q6E0V2)
brenda
Bailey, M.E.; Sackett, D.L.; Ross, J.L.
Katanin severing and binding microtubules are inhibited by tubulin carboxy tails
Biophys. J.
109
2546-2561
2015
Homo sapiens (O75449), Homo sapiens, Xenopus laevis (Q9PUL2)
brenda
Joly, N.; Martino, L.; Gigant, E.; Dumont, J.; Pintard, L.
Microtubule-severing activity of the AAA+ ATPase Katanin is essential for female meiotic spindle assembly
Development
143
3604-3614
2016
Caenorhabditis elegans (P34808), Caenorhabditis elegans
brenda
Fan, X.; Lin, Z.; Fan, G.; Lu, J.; Hou, Y.; Habai, G.; Sun, L.; Yu, P.; Shen, Y.; Wen, M.; Wang, C.
The AAA protein spastin possesses two levels of basal ATPase activity
FEBS Lett.
592
1625-1633
2018
Homo sapiens (Q9UBP0)
brenda
Luptovciak, I.; Samakovli, D.; Komis, G.; Samaj, J.
KATANIN 1 is essential for embryogenesis and seed formation in Arabidopsis
Front. Plant Sci.
8
728
2017
Arabidopsis thaliana (Q9SEX2), Arabidopsis thaliana ecotype Columbia (Q9SEX2)
brenda
Nithianantham, S.; McNally, F.J.; Al-Bassam, J.
Structural basis for disassembly of katanin heterododecamers
J. Biol. Chem.
293
10590-10605
2018
Caenorhabditis elegans (P34808), Homo sapiens (Q9BW62)
brenda
Cheung, K.; Senese, S.; Kuang, J.; Bui, N.; Ongpipattanakul, C.; Gholkar, A.; Cohn, W.; Capri, J.; Whitelegge, J.P.; Torres, J.Z.
Proteomic analysis of the mammalian Katanin family of microtubule-severing enzymes defines Katanin p80 subunit B-like 1 (KATNBL1) as a regulator of mammalian Katanin microtubule-severing
Mol. Cell. Proteomics
15
1658-1669
2016
Homo sapiens (Q9BW62)
brenda
Waclawek, E.; Joachimiak, E.; Hall, M.H.; Fabczak, H.; Wloga, D.
Regulation of katanin activity in the ciliate Tetrahymena thermophila
Mol. Microbiol.
103
134-150
2017
Tetrahymena thermophila, Tetrahymena thermophila CU428.2
brenda
Grode, K.D.; Rogers, S.L.
The non-catalytic domains of Drosophila katanin regulate its abundance and microtubule-disassembly activity
PLoS ONE
10
e0123912
2015
Drosophila melanogaster (Q9VN89)
brenda
Abu-Abied, M.; Mordehaev, I.; Sunil Kumar, G.B.; Ophir, R.; Wasteneys, G.O.; Sadot, E.
Analysis of microtubule-associated-proteins during IBA-mediated adventitious root induction reveals KATANIN dependent and independent aterations of expression patterns
PLoS ONE
10
e0143828
2015
Arabidopsis thaliana (Q9SEX2), Arabidopsis thaliana ecotype Columbia (Q9SEX2)
brenda
Rezabkova, L.; Jiang, K.; Capitani, G.; Prota, A.E.; Akhmanova, A.; Steinmetz, M.O.; Kammerer, R.A.
Structural basis of katanin p60 p80 complex formation
Sci. Rep.
7
14893
2017
Mus musculus (Q9WV86 AND Q8BG40)
brenda
Jiang, K.; Faltova, L.; Hua, S.; Capitani, G.; Prota, A.E.; Landgraf, C.; Volkmer, R.; Kammerer, R.A.; Steinmetz, M.O.; Akhmanova, A.
Structural basis of formation of the microtubule minus-end-regulating CAMSAP-Katanin complex
Structure
26
375-382.e4
2018
Mus musculus
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 5.6.1.1)
Transporter Classification Database (TCDB): 1.R.1.1.1
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
