%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 }