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J. Biol. Chem., Vol. 277, Issue 36, 32413-32416, September 6, 2002

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Jab1 Co-activation of c-Jun Is Abrogated by the Serine 10-phosphorylated Form of p27^Kip1*

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

From the  Department of Biological Sciences, Imperial College of Science, Technology and Medicine, Exhibition Road, South Kensington, London SW7 2AY and ^§ Department of Cancer Medicine, Cancer Research-United Kingdom Laboratories and Section of Cancer Cell Biology, MRC Cyclotron Building, Imperial College School of Medicine at Hammersmith Hospital, Du Cane Road, London W12 0NN, United Kingdom

The cyclin-dependent kinase (cdk) inhibitor p27^Kip1 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 p27^Kip1 levels. Jab1 has been reported to interact with p27^Kip1 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 p27^Kip1 at serine 10 leads to the suppression of Jab1 levels with the concomitant inhibition of c-Jun-dependent transcription. This repression is minimized upon quiescence exit through the rapid and preferential loss of the serine 10-phosphorylated form of p27^Kip1 following serum stimulation. Our results, therefore, demonstrate an additional role for p27^Kip1 in the modulation of c-Jun-dependent transcription via Jab1.

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