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J. Biol. Chem., Vol. 277, Issue 17, 14355-14358, April 26, 2002
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§,§,§,
, and§**
From the Departments of Phosphorylation of the
cyclin-dependent kinase inhibitor
p27Kip1 has been thought to regulate its
stability. Ser10 is the major phosphorylation site of
p27Kip1, and phosphorylation of this residue
affects protein stability. Phosphorylation of
p27Kip1 on Ser10 has now been shown
to be required for the binding of CRM1, a carrier protein for nuclear
export. The p27Kip1 protein was translocated
from the nucleus to the cytoplasm at the G0-G1
transition of the cell cycle, and this export was inhibited by
leptomycin B, a specific inhibitor of CRM1-dependent
nuclear export. The nuclear export and subsequent degradation of
p27Kip1 at the G0-G1
transition were observed in cells lacking Skp2, the F-box protein
component of an SCF ubiquitin ligase complex, indicating that these
early events are independent of Skp2-mediated proteolysis. Substitution
of Ser10 with Ala (S10A) markedly reduced the extent of
p27Kip1 export, whereas substitution of
Ser10 with Asp (S10D) or Glu (S10E) promoted export.
Co-immunoprecipitation analysis showed that CRM1 preferentially
interacted with S10D and S10E but not with S10A, suggesting that the
phosphorylation of p27Kip1 on Ser10
is required for its binding to CRM1 and for its subsequent nuclear export.
Molecular and Cellular
Biology and Molecular Genetics, Medical Institute of
Bioregulation, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka,
Fukuoka 812-8582, Japan, § Core Research for Evolutional
Science and Technology (CREST), Japan Science and Technology
Corporation, 4-1-8 Honcho, Kawaguchi, Saitama 332-0012, Japan, and the
¶ Department of Biotechnology, Graduate School of Agriculture and
Life Sciences, University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo
113-8657, Japan
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