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M603439200v1
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Papers In Press, published online ahead of print April 13, 2006
J. Biol. Chem, 10.1074/jbc.M603439200
Submitted on April 10, 2006
Accepted on April 13, 2006

Cyclin D1-Cdk4 induce Runx2 ubiquitination and degradation

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

Orthopaedics Dept., University of Rochester, Rochester, NY 14642

Corresponding Author: di_chen{at}urmc.rochester.edu

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. Here 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.


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