Article
Phosphorylation at serine 10, a major phosphorylation site of p27(Kip1), increases its protein stability.
The Journal of biological chemistry - 18 Aug 2000
Ishida N, Kitagawa M, Hatakeyama S, Nakayama K
Abstract excerpt
The association of the p27(Kip1) protein with cyclin and cyclin-dependent kinase complexes inhibits their kinase activities and contributes to the control of cell proliferation. The p27(Kip1) protein has now been shown to be phosphorylated in vivo, and this phosphorylation reduces the electrophoretic mobility of the protein. Substitution of Ser(10) with Ala (S10A) markedly reduced the extent of p27(Kip1)...
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