[HTML][HTML] Role of serine 10 phosphorylation in p27 stabilization revealed by analysis of p27 knock-in mice harboring a serine 10 mutation
Y Kotake, K Nakayama, N Ishida… - Journal of Biological …, 2005 - ASBMB
The inhibition of cyclin-dependent kinase activity by p27 contributes to regulation of cell
cycle progression. Serine 10 is the major phosphorylation site of p27, and its
phosphorylation has been shown to affect the stability and nuclear export of p27 at the G 0-G
1 transition in transfected cultured cells. To investigate the physiological relevance of p27
phosphorylation on Ser 10, we generated p27" knock-in" mice that harbor an S10A mutation
in this protein. Mice homozygous for the mutation (p27 S10A/S10A mice) were normal in …
cycle progression. Serine 10 is the major phosphorylation site of p27, and its
phosphorylation has been shown to affect the stability and nuclear export of p27 at the G 0-G
1 transition in transfected cultured cells. To investigate the physiological relevance of p27
phosphorylation on Ser 10, we generated p27" knock-in" mice that harbor an S10A mutation
in this protein. Mice homozygous for the mutation (p27 S10A/S10A mice) were normal in …