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Related Experiment Videos

Proteolysis and the cell cycle: with this RING I do thee destroy.

M Tyers1, P Jorgensen

  • 1Programme in Molecular Biology and Cancer, Graduate Department of Molecular and Medical Genetics, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, University of Toronto, Toronto, M5G 1X5, M5S 1A8, Canada. tyers@mshri.on.ca.

Current Opinion in Genetics & Development
|February 19, 2000
PubMed
Summary

The ubiquitin system controls cell division by degrading regulatory proteins. Key E3 ligase complexes, SCF and APC/C, form a master oscillator coordinating genome replication and segregation.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • The ubiquitin system is crucial for regulating the cell division cycle.
  • Timely destruction of regulatory proteins is essential for cell cycle progression.

Purpose of the Study:

  • To identify and characterize the E3 ubiquitin ligase superfamilies involved in cell cycle control.
  • To elucidate the regulatory circuits coordinating cell cycle events.

Main Methods:

  • Analysis of Skp1-Cdc53/cullin-F-box protein (SCF) complexes.
  • Investigation of the anaphase-promoting complex/cyclosome (APC/C).
  • Studying the interconnection of SCF, APC/C, and cyclin-dependent kinase activities.

Main Results:

Related Experiment Videos

  • SCF and APC/C complexes represent a new superfamily of E3 ubiquitin ligases.
  • These ligases share common cullin and RING-H2 finger protein subunits.
  • Interconnected circuits of SCF, APC/C, and cyclin-dependent kinases form a master cell cycle oscillator.

    • Conclusions:

    • The ubiquitin system, through SCF and APC/C, plays a central role in cell cycle progression.
    • These E3 ligases are key components of a master oscillator that ensures accurate genome replication and segregation.