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A more recent version of this article appeared on June 15, 2001
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Papers In Press, published online ahead of print April 17, 2001
J. Biol. Chem, 10.1074/jbc.M009388200
Submitted on October 13, 2000
Revised on March 29, 2001
Accepted on April 17, 2001

The nuclear ubiquitin-proteasome system degrades MyoD

Z Elizabeth Floyd, Julia S. Trausch-Azar, Eyal Reinstein, Aaron Ciechanover, and Alan L. Schwartz

Department of Pediatrics, Washington University School of Medicine, St. Louis, MO 63110

Corresponding Author: schwartz{at}kids.wustl.edu

Many short-lived nuclear proteins are targeted for degradation by the ubiquitin-proteasome pathway. The role of the nucleus in regulating the turnover of these proteins is not well defined, although many components of the ubiquitin-proteasome system are localized in the nucleus. We have used nucleoplasm from highly purified HeLa nuclei to examine the degradation of a physiological substrate of the ubiquitin-proteasome system (MyoD). In vitro studies using inhibitors of the system demonstrate MyoD is degraded via the ubiquitin-proteasome pathway in HeLa nucleoplasm. Purified nucleoplasm in vitro also supports the generation of high molecular mass MyoD-ubiquitin adducts. In addition, in vivo studies using leptomycin B to inhibit nuclear export, demonstrate that MyoD is degraded in HeLa cells by the nuclear ubiquitin-proteasome system.


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