Abstract
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.
Publication types
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Anaphase-Promoting Complex-Cyclosome
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Animals
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Cell Cycle / physiology*
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Cell Division
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Cyclin-Dependent Kinases / metabolism
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Homeostasis
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Humans
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Ligases / metabolism
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Saccharomyces cerevisiae / cytology
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / physiology
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Saccharomyces cerevisiae Proteins
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Ubiquitin-Conjugating Enzymes
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Ubiquitin-Protein Ligase Complexes*
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Ubiquitin-Protein Ligases
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Ubiquitins / metabolism*
Substances
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Saccharomyces cerevisiae Proteins
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Ubiquitins
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CDC34 protein, S cerevisiae
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CDC34 protein, human
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Ubiquitin-Conjugating Enzymes
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Ubiquitin-Protein Ligase Complexes
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Anaphase-Promoting Complex-Cyclosome
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Ubiquitin-Protein Ligases
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Cyclin-Dependent Kinases
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Ligases