Open AccessHuman p53 is phosphorylated by p60-cdc2 and cyclin B-cdc2.
Author(s) -
James R. Bischoff,
Paula N. Friedman,
Daniel R. Marshak,
Carol Prives,
David Beach
Publication year - 1990
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.87.12.4766
Subject(s) - cyclin dependent kinase 1 , phosphorylation , cell cycle , serine , cyclin a , cyclin b1 , phosphorylation cascade , protein phosphorylation , cyclin b , microbiology and biotechnology , biology , chemistry , biochemistry , cyclin , protein kinase a , cell
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.