Phosphorylation of p27Kip1 on serine 10 is required for its binding to CRM1 and nuclear export
N Ishida, T Hara, T Kamura, M Yoshida… - Journal of Biological …, 2002 - ASBMB
Phosphorylation of the cyclin-dependent kinase inhibitor p27 Kip1 has been thought to
regulate its stability. Ser 10 is the major phosphorylation site of p27 Kip1, and
phosphorylation of this residue affects protein stability. Phosphorylation of p27 Kip1 on Ser
10 has now been shown to be required for the binding of CRM1, a carrier protein for nuclear
export. The p27 Kip1 protein was translocated from the nucleus to the cytoplasm at the G 0-
G 1 transition of the cell cycle, and this export was inhibited by leptomycin B, a specific …
regulate its stability. Ser 10 is the major phosphorylation site of p27 Kip1, and
phosphorylation of this residue affects protein stability. Phosphorylation of p27 Kip1 on Ser
10 has now been shown to be required for the binding of CRM1, a carrier protein for nuclear
export. The p27 Kip1 protein was translocated from the nucleus to the cytoplasm at the G 0-
G 1 transition of the cell cycle, and this export was inhibited by leptomycin B, a specific …
