{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,5]],"date-time":"2026-02-05T09:50:28Z","timestamp":1770285028873,"version":"3.49.0"},"reference-count":45,"publisher":"Wiley","issue":"8","license":[{"start":{"date-parts":[[2015,6,10]],"date-time":"2015-06-10T00:00:00Z","timestamp":1433894400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J of Cellular Biochemistry"],"published-print":{"date-parts":[[2015,8]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:sec><jats:label\/><jats:p>Wip1 belongs to the protein phosphatase C (PP2C) family, of which expression is up\u2010regulated by a number of external stresses, and serves as a stress modulator in normal physiological conditions. When overexpressed, premature dephosphorylation of stress\u2010mediators by Wip1 results in abrogation of tumor surveillance, thus Wip1 acts as an oncogene. Previously, the functional regulation of Wip1 in cell\u2010cycle progression by counteracting cellular G1 and G2\/M checkpoint activity in response to DNA damage was reported. However, other than in stress conditions, the function and regulatory mechanism of Wip1 has not been fully determined. Herein, we demonstrated that protein regulation of Wip1 occurs in a cell cycle\u2010dependent manner, which is directly governed by APC\/C<jats:sup>Cdh1<\/jats:sup> at the end of mitosis. In particular, we also showed evidence that Wip1 phosphatase activity is closely associated with its own protein stability, suggesting that reduced phosphatase activity of Wip1 during mitosis could trigger its degradation. Furthermore, to verify the physiological role of its phosphatase activity during mitosis, we established doxycycline\u2010inducible cell models, including a Wip1 wild type (WT) and phosphatase dead mutant (Wip1 DA). When ectopically expressing Wip1 WT, we observed a delay in the transition from metaphase to anaphase. In conclusion, these studies show that mitotic degradation of Wip1 by APC\/C<jats:sup>Cdh1<\/jats:sup> is important for normal mitotic progression. J. Cell. Biochem. 116: 1602\u20131612, 2015. \u00a9 2015 Wiley Periodicals, Inc.<\/jats:p><\/jats:sec>","DOI":"10.1002\/jcb.25114","type":"journal-article","created":{"date-parts":[[2015,2,3]],"date-time":"2015-02-03T22:33:19Z","timestamp":1423002799000},"page":"1602-1612","source":"Crossref","is-referenced-by-count":18,"title":["Timely Degradation of Wip1 Phosphatase by APC\/C Activator Protein Cdh1 is Necessary for Normal Mitotic Progression"],"prefix":"10.1002","volume":"116","author":[{"given":"Ho\u2010Chang","family":"Jeong","sequence":"first","affiliation":[{"name":"College of Natural Sciences Department of Life Sciences Sogang University Seoul Korea"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Na\u2010Yeon","family":"Gil","sequence":"additional","affiliation":[{"name":"College of Natural Sciences Department of Life Sciences Sogang University Seoul 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