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A more recent version of this article appeared on August 30, 2002
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C200311200v1
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Papers In Press, published online ahead of print July 15, 2002
J. Biol. Chem, 10.1074/jbc.C200311200
Submitted on May 20, 2002
Revised on July 12, 2002
Accepted on July 14, 2002

Jab1 co-activation of c-Jun is abrogated by the serine 10 phosphorylated form of p27Kip1

Shalu Chopra, Silvia Fernandez de Mattos, Eric W.-F. Lam, and David J. Mann

Department of Biological Sciences, Imperial College, London SW7 2AY

Corresponding Author: d.mann{at}ic.ac.uk

The cyclin-dependent kinase (cdk) inhibitor p27Kip1 is a central mediator in the imposition and maintenance of quiescence through the sequestration of G1-specific cyclin/cdk complexes. Previous studies have implicated the c-Jun co-activator protein Jab1 as a regulator of intracellular p27Kip1 levels. Jab1 has been reported to interact with p27Kip1 and cause its translocation to the cytoplasm as a prelude to the degradation of the cdk inhibitor. Here we describe experiments that showing phosphorylation of p27Kip1 at serine 10 leads to the suppression of Jab1 levels with the concomitant inhibition of c-Jun-dependent transcription. This repression is minimised upon quiescence exit through the rapid and preferential loss of the serine 10 phosphorylated form of p27Kip1 following serum stimulation. Our results, therefore, demonstrate an additional role for p27Kip1 in the modulation of c-Jun-dependent transcription via Jab1.


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