Journal
NATURE CELL BIOLOGY
Volume 7, Issue 1, Pages 21-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncb1201
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Funding
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM039434, R01GM044428] Funding Source: NIH RePORTER
- NIGMS NIH HHS [GM39434, GM44428] Funding Source: Medline
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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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