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Altered states: programmed proteolysis and the budding yeast cell cycle.

P Jorgensen¹, M Tyers

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.

Current Opinion in Microbiology

|December 23, 1999

Summary

Scientists discovered a new E3 ubiquitin ligase enzyme family. This includes the anaphase-promoting complex (APC), which controls cell division through proteolysis and phosphatase activity, driving mitosis exit.

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Area of Science:

Cell Biology
Molecular Biology
Biochemistry

Background:

The SCF E3 ubiquitin ligase complex is essential in budding yeast.
Related E3 enzymes, including the anaphase-promoting complex (APC), are crucial for cell cycle progression.

Purpose of the Study:

To explore the functional insights into APC-dependent proteolysis.
To understand the mechanisms regulating mitosis exit.

Main Methods:

Identification of an essential RING-H2 finger protein in the SCF complex.
Analysis of APC-dependent proteolysis and phosphatase activity.

Main Results:

Uncovered a family of related E3 enzymes, including the APC.
Identified novel protease activity dissolving sister chromatid cohesion at anaphase.

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Demonstrated that Cdc14 phosphatase release eliminates cyclin-dependent kinase activity, driving mitosis exit.

Conclusions:

The APC plays a critical role in cell cycle regulation.
APC-dependent proteolysis and phosphatase activity are key to mitotic exit.