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Human p53 is phosphorylated by p60-cdc2 and cyclin B-cdc2.
Howard Hughes Medical Institute, Cold Spring Harbor Laboratory, NY 11724.
The human anti-oncoprotein p53 is shown to be a substrate of cdc2. The primary site of phosphorylation is serine-315. Serine-315 is phosphorylated by both p60-cdc2 and cyclin B-cdc2 enzymes. The phosphorylation of p53 is cell cycle-dependent. The abundance of p53 also oscillates during the cell cycle. The protein is largely absent from cells that have just completed division but accumulates in cells during G1 phase. Phosphorylation by cdc2 might regulate the antiproliferative activity of p53.
PMID: 2141171 [PubMed - indexed for MEDLINE]
PMCID: PMC54198
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Cited by 68 PubMed Central articles
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Cell cycle-dependent nuclear retention of p53 by E2F1 requires phosphorylation of p53 at Ser315.
Fogal V, Hsieh JK, Royer C, Zhong S, Lu X.
EMBO J. 2005 Aug 3; 24(15):2768-82. Epub 2005 Jul 21.
[EMBO J. 2005]
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Endoplasmic reticulum stress induces p53 cytoplasmic localization and prevents p53-dependent apoptosis by a pathway involving glycogen synthase kinase-3beta.
Qu L, Huang S, Baltzis D, Rivas-Estilla AM, Pluquet O, Hatzoglou M, Koumenis C, Taya Y, Yoshimura A, Koromilas AE.
Genes Dev. 2004 Feb 1; 18(3):261-77. Epub 2004 Jan 26.
[Genes Dev. 2004]
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A novel RING finger protein, human enhancer of invasion 10, alters mitotic progression through regulation of cyclin B levels.
Toby GG, Gherraby W, Coleman TR, Golemis EA.
Mol Cell Biol. 2003 Mar; 23(6):2109-22.
[Mol Cell Biol. 2003]
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