کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2108081 | 1083720 | 2008 | 12 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: GSK-3β Targets Cdc25A for Ubiquitin-Mediated Proteolysis, and GSK-3β Inactivation Correlates with Cdc25A Overproduction in Human Cancers GSK-3β Targets Cdc25A for Ubiquitin-Mediated Proteolysis, and GSK-3β Inactivation Correlates with Cdc25A Overproduction in Human Cancers](/preview/png/2108081.png)
SummaryThe Cdc25A phosphatase positively regulates cell-cycle transitions, is degraded by the proteosome throughout interphase and in response to stress, and is overproduced in human cancers. The kinases targeting Cdc25A for proteolysis during early cell-cycle phases have not been identified, and mechanistic insight into the cause of Cdc25A overproduction in human cancers is lacking. Here, we demonstrate that glycogen synthase kinase-3β (GSK-3β) phosphorylates Cdc25A to promote its proteolysis in early cell-cycle phases. Phosphorylation by GSK-3β requires priming of Cdc25A, and this can be catalyzed by polo-like kinase 3 (Plk-3). Importantly, a strong correlation between Cdc25A overproduction and GSK-3β inactivation was observed in human tumor tissues, indicating that GSK-3β inactivation may account for Cdc25A overproduction in a subset of human tumors.
Journal: - Volume 13, Issue 1, 8 January 2008, Pages 36–47