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The FASEB Journal, Vol 11, 1067-1075, Copyright © 1997 by The Federation of American Societies for Experimental Biology

REVIEWS

Cell cycle regulation by the ubiquitin pathway

M Pagano
Department of Pathology and Kaplan Cancer Center, New York University Medical Center, New York 10016, USA.

In the past 2 years, two ubiquitin-dependent proteolytic pathways have been established as important players in the regulation of the cell division cycle. In S. cerevisiae, the entry into S phase requires ubiquitin-mediated degradation of a cdk inhibitor, p40Sic1, in a pathway that involves the E2 enzyme Cdc34. Recent studies reviewed herein show that the Cdc34 pathway targets phosphorylated substrates. A second pathway that regulates chromosome segregation and mitotic exit by degrading anaphase inhibitors and mitotic cyclins involves a different E2 and a large molecular weight E3 complex, called the anaphase-promoting complex or cyclosome. This pathway targets substrates containing one or more destruction box motif.


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