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Related Experiment Videos

Cell cycle regulation by the ubiquitin pathway

M Pagano1

  • 1Department of Pathology and Kaplan Cancer Center, New York University Medical Center, New York 10016, USA.

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
|November 21, 1997
PubMed
Summary

Two ubiquitin-dependent pathways regulate the cell division cycle. One pathway uses the Cdc34 E2 enzyme to degrade phosphorylated substrates for S phase entry, while another targets destruction boxes for cell cycle progression.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Ubiquitin-dependent proteolysis is crucial for cell cycle regulation.
  • Two key pathways have emerged in regulating cell division.

Purpose of the Study:

  • To review the established ubiquitin-dependent proteolytic pathways involved in cell cycle control.
  • To highlight the mechanisms and substrates targeted by these pathways.

Main Methods:

  • Review of recent studies on ubiquitin-mediated protein degradation.
  • Analysis of the roles of E2 enzymes and E3 complexes in cell cycle regulation.

Main Results:

  • The Cdc34 E2 enzyme pathway degrades phosphorylated substrates, like p40Sic1, enabling S phase entry in S. cerevisiae.

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  • A second pathway, involving the anaphase-promoting complex/cyclosome, degrades anaphase inhibitors and mitotic cyclins via destruction box motifs to regulate chromosome segregation and mitotic exit.
  • Conclusions:

    • Ubiquitin-dependent proteolysis plays a vital role in precise cell cycle progression.
    • Distinct ubiquitinylation pathways target specific substrates to control critical cell division events.