Cell cycle regulation by the ubiquitin pathway.
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.
Pagano
M
M
Department of Pathology and Kaplan Cancer Center, New York University Medical Center, New York 10016, USA.
D064173:Anaphase-Promoting Complex-Cyclosome; D000818:Animals; D002453:Cell Cycle / Q000502:physiology*; D002455:Cell Division; D018844:Cyclin-Dependent Kinases / Q000378:metabolism; D006706:Homeostasis; D006801:Humans; D008025:Ligases / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000166:cytology / Q000235:genetics / Q000502:physiology; D029701:Saccharomyces cerevisiae Proteins; D044763:Ubiquitin-Conjugating Enzymes; D043743:Ubiquitin-Protein Ligase Complexes; D044767:Ubiquitin-Protein Ligases; D014452:Ubiquitins / Q000378:metabolism*
D029701:Saccharomyces cerevisiae Proteins; D014452:Ubiquitins; C577449:CDC34 protein, S cerevisiae; C577447:CDC34 protein, human; D044763:Ubiquitin-Conjugating Enzymes; D043743:Ubiquitin-Protein Ligase Complexes; D064173:Anaphase-Promoting Complex-Cyclosome; D044767:Ubiquitin-Protein Ligases; D018844:Cyclin-Dependent Kinases; D008025:Ligases