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J. Biol. Chem., Vol. 281, Issue 24, 16347-16353, June 16, 2006

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Cyclin D1-Cdk4 Induce Runx2 Ubiquitination and Degradation^*

Run Shen, Xiumei Wang, Hicham Drissi, Fang Liu, Regis J. O'Keefe, and Di Chen¹

From the Department of Orthopaedics, Center for Musculoskeletal Research, University of Rochester School of Medicine, Rochester, New York 14642 and the Center for Advanced Biotechnology and Medicine, Rutgers, the State University of New Jersey, Piscataway, New Jersey 08854

Runx2 is a Runt domain transcription factor involved in the activation of genes encoding osteoblast and chondrocyte-specific proteins. Runx2 activity is regulated by transcriptional and post-transcriptional mechanisms. The functional significance of the post-translational modification of Runx2 has not been fully defined. We show that cyclin D1-Cdk4 induce Runx2 degradation in an ubiquitination-proteasome-dependent manner. Mutagenesis of Runx2 serine-472, a consensus Cdk site, to alanine increases the half-life of Runx2 and causes loss of sensitivity to cyclin D1-induced Runx2 degradation. The targeted Runx2 degradation by cyclin D1 identifies a novel mechanism through which Runx2 activity is regulated coordinately with the cell cycle machinery in bone cells.

Received for publication, April 10, 2006

^* This work was supported by Grants AR051189 and AR048920 (to D. C.) and Grant AR38945 (to R. J. O.) from the National Institutes of Health. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed. Fax: 585-275-1121; E-mail: di_chen{at}urmc.rochester.edu.

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