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Nat Cell Biol. 2005 Jan;7(1):21-9. Epub 2004 Dec 5.

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

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The Scripps Research Institute, Departments of Immunology and Cell Biology, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.


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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