Chronophin, a novel HAD-type serine protein phosphatase, regulates
cofilin-dependent actin dynamics
A. Gohla, J. Birkenfeld, und G. Bokoch. Nat Cell Biol, 7 (1):
21-9(Januar 2005)Gohla, Antje Birkenfeld, Jorg Bokoch, Gary M GM39434/GM/NIGMS NIH
HHS/United States GM44428/GM/NIGMS NIH HHS/United States Research
Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. England
Nature cell biology Nat Cell Biol. 2005 Jan;7(1):21-9. Epub 2004
Dec 5..
Cofilin is a key regulator of actin cytoskeletal dynamics whose activity
is controlled by phosphorylation of a single serine residue. We report
the biochemical isolation of chronophin (CIN), a unique cofilin-activating
phosphatase of the haloacid dehalogenase (HAD) superfamily. CIN directly
dephosphorylates cofilin with high specificity and colocalizes with
cofilin in motile and dividing cells. Loss of CIN activity blocks
phosphocycling of cofilin, stabilizes F-actin structures and causes
massive cell division defects. Our findings identify a physiological
phospho-serine protein substrate for a mammalian HAD-type phosphatase
and demonstrate that CIN is an important novel regulator of cofilin-mediated
actin reorganization.
Gohla, Antje Birkenfeld, Jorg Bokoch, Gary M GM39434/GM/NIGMS NIH
HHS/United States GM44428/GM/NIGMS NIH HHS/United States Research
Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. England
Nature cell biology Nat Cell Biol. 2005 Jan;7(1):21-9. Epub 2004
Dec 5.
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%0 Journal Article
%1 Gohla2005
%A Gohla, A.
%A Birkenfeld, J.
%A Bokoch, G. M.
%D 2005
%J Nat Cell Biol
%K & Acid Actin Actins/*metabolism Amino Animals Base Cell Complementary/analysis/genetics Cycle Cytoplasm/metabolism DNA, Data Depolymerizing Division/physiology Down-Regulation/physiology Factors Gohla Hela Humans Hydrolases/chemistry/*metabolism Interference Microfilament Microfilaments/*metabolism Molecular Movement/physiology Phosphatases/genetics/isolation Phosphoprotein Phosphorylation Proteins/genetics/isolation Pseudopodia/metabolism RNA Rabbits Sequence Serine/metabolism purification/*metabolism purification/metabolism Proteins/metabolism
%N 1
%P 21-9
%T Chronophin, a novel HAD-type serine protein phosphatase, regulates
cofilin-dependent actin dynamics
%U http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15580268
%V 7
%X Cofilin is a key regulator of actin cytoskeletal dynamics whose activity
is controlled by phosphorylation of a single serine residue. We report
the biochemical isolation of chronophin (CIN), a unique cofilin-activating
phosphatase of the haloacid dehalogenase (HAD) superfamily. CIN directly
dephosphorylates cofilin with high specificity and colocalizes with
cofilin in motile and dividing cells. Loss of CIN activity blocks
phosphocycling of cofilin, stabilizes F-actin structures and causes
massive cell division defects. Our findings identify a physiological
phospho-serine protein substrate for a mammalian HAD-type phosphatase
and demonstrate that CIN is an important novel regulator of cofilin-mediated
actin reorganization.
@article{Gohla2005,
abstract = {Cofilin is a key regulator of actin cytoskeletal dynamics whose activity
is controlled by phosphorylation of a single serine residue. We report
the biochemical isolation of chronophin (CIN), a unique cofilin-activating
phosphatase of the haloacid dehalogenase (HAD) superfamily. CIN directly
dephosphorylates cofilin with high specificity and colocalizes with
cofilin in motile and dividing cells. Loss of CIN activity blocks
phosphocycling of cofilin, stabilizes F-actin structures and causes
massive cell division defects. Our findings identify a physiological
phospho-serine protein substrate for a mammalian HAD-type phosphatase
and demonstrate that CIN is an important novel regulator of cofilin-mediated
actin reorganization.},
added-at = {2010-12-14T18:12:02.000+0100},
author = {Gohla, A. and Birkenfeld, J. and Bokoch, G. M.},
biburl = {https://www.bibsonomy.org/bibtex/20e401f3a67256aca098edb41effeb4bb/pharmawuerz},
endnotereftype = {Journal Article},
interhash = {6ef34c2216272fcc9971790ca81a6a10},
intrahash = {0e401f3a67256aca098edb41effeb4bb},
issn = {1465-7392 (Print) 1465-7392 (Linking)},
journal = {Nat Cell Biol},
keywords = {& Acid Actin Actins/*metabolism Amino Animals Base Cell Complementary/analysis/genetics Cycle Cytoplasm/metabolism DNA, Data Depolymerizing Division/physiology Down-Regulation/physiology Factors Gohla Hela Humans Hydrolases/chemistry/*metabolism Interference Microfilament Microfilaments/*metabolism Molecular Movement/physiology Phosphatases/genetics/isolation Phosphoprotein Phosphorylation Proteins/genetics/isolation Pseudopodia/metabolism RNA Rabbits Sequence Serine/metabolism purification/*metabolism purification/metabolism Proteins/metabolism},
month = Jan,
note = {Gohla, Antje Birkenfeld, Jorg Bokoch, Gary M GM39434/GM/NIGMS NIH
HHS/United States GM44428/GM/NIGMS NIH HHS/United States Research
Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. England
Nature cell biology Nat Cell Biol. 2005 Jan;7(1):21-9. Epub 2004
Dec 5.},
number = 1,
pages = {21-9},
shorttitle = {Chronophin, a novel HAD-type serine protein phosphatase, regulates
cofilin-dependent actin dynamics},
timestamp = {2010-12-14T18:21:42.000+0100},
title = {Chronophin, a novel HAD-type serine protein phosphatase, regulates
cofilin-dependent actin dynamics},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15580268},
volume = 7,
year = 2005
}