Journal
CELL CYCLE
Volume 5, Issue 12, Pages 1313-1319Publisher
TAYLOR & FRANCIS INC
DOI: 10.4161/cc.5.12.2863
Keywords
Akt/PKB; p21 Cip1 Waf1 Sdi1; cyclin; cdk; cell cycle; phosphorylation; degradation; protein/protein interaction; PKC; p27 Kip1
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Funding
- Biotechnology and Biological Sciences Research Council [BB/C508134/1] Funding Source: researchfish
- Biotechnology and Biological Sciences Research Council [BB/C508134/1] Funding Source: Medline
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p21 was originally described as functioning as a cell cycle regulator via inhibition of both cyclin-dependent kinases and processive DNA replication. Nowadays it is recognized to play other fundamental roles including transcriptional regulation and the modulation of apoptosis. Each of these functions of p21 is achieved through direct p21/protein interactions and the subcellular localization of p21 plays an important part in dictating the binding partners to which p21 is exposed. Over recent years, a number of phosphorylation sites in p21 have been identified, these being targeted by several important intracellular signalling protein kinases. Here we review the state of our knowledge of p21 phosphorylation with respect to the kinases involved and the molecular biological effects of each phosphorylation event.
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