Journal
CANCER CELL
Volume 13, Issue 1, Pages 36-47Publisher
CELL PRESS
DOI: 10.1016/j.ccr.2007.12.002
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Funding
- NATIONAL CANCER INSTITUTE [ZIABC005599] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM047017] Funding Source: NIH RePORTER
- NIGMS NIH HHS [R01 GM047017-17, R01 GM047017, R01 GM047017-16] Funding Source: Medline
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The 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-3 beta (GSK-3 beta) phosphorylates Cdc25A to promote its proteolysis in early cell-cycle phases. Phosphorylation by GSK-3 beta requires priming of Cdc25A, and this can be catalyzed by polo-like kinase 3 (PIk-3). Importantly, a strong correlation between Cdc25A overproduction and GSK-3 beta inactivation was observed in human tumor tissues, indicating that GSK-3 beta inactivation may account for Cdc25A overproduction in a subset of human tumors.
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