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Reversible tyrosine phosphorylation and cell cycle control
S Atherton-Fessler1, G Hannig, H Piwnica-Worms
1Department of Physiology, Tufts University School of Medicine, Boston, MA 02111.
Seminars in Cell Biology
|December 1, 1993
Summary
Reversible tyrosine phosphorylation controls cell division entry. Key protein kinases (wee1, mik1, cdr1) and phosphatases (cdc25, pyp1-3) in fission yeast regulate p34cdc2 activity, a crucial step for mitosis.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Reversible tyrosine phosphorylation regulates eukaryotic cell growth and the cell division cycle.
- The protein kinase p34cdc2 activity, essential for mitosis entry, is controlled by tyrosine 15 phosphorylation.
- Protein kinases and phosphatases form a network regulating p34cdc2 phosphorylation and cell cycle progression.
Purpose of the Study:
- To review the roles of key protein kinases and phosphatases in regulating cell division.
- To highlight the genetic approaches used in fission yeast to identify these regulators.
- To underscore the conserved nature of tyrosine phosphorylation in cell cycle control across eukaryotes.
Main Methods:
- Genetic approaches in Schizosaccharomyces pombe to identify genes encoding cell cycle regulators.
- Focus on specific protein kinases: wee1+, mik1+, cdr1+/nim1+.
- Focus on specific protein phosphatases: cdc25+, pyp1+, pyp2+, pyp3+.
Main Results:
- Identification of several key protein kinases and phosphatases involved in p34cdc2 regulation.
- Demonstration of a complex regulatory network controlling tyrosine phosphorylation.
- Evidence for conserved mechanisms of cell cycle regulation in higher eukaryotes.
Conclusions:
- Reversible tyrosine phosphorylation is a fundamental mechanism for cell division cycle control.
- The identified kinases and phosphatases play critical roles in regulating mitosis entry.
- Conserved regulators highlight the universal importance of this phosphorylation-based system.