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Publication : Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics.

First Author  Gohla A Year  2005
Journal  Nat Cell Biol Volume  7
Issue  1 Pages  21-9
PubMed ID  15580268 Mgi Jnum  J:337085
Mgi Id  MGI:7493898 Doi  10.1038/ncb1201
Citation  Gohla A, et al. (2005) Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics. Nat Cell Biol 7(1):21-9
abstractText  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.
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