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Negative regulation of mitosis by two functionally overlapping PTPases in fission yeast

J B Millar1, P Russell, J E Dixon

  • 1Department of Molecular, Scripps Research Institute, La Jolla, CA 92037.

The EMBO Journal
|December 1, 1992
PubMed

Insights

A new protein tyrosine phosphatase (PTPase) gene, pyp2, was found in fission yeast. It works with pyp1 to control mitosis onset, revealing a new role for protein tyrosine phosphorylation in cell division.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Genetics

Background:

  • Fission yeast is a model organism for studying cell cycle control.
  • Protein tyrosine phosphatases (PTPases) are enzymes that remove phosphate groups from tyrosine residues.
  • Mitosis is a crucial process for cell division, regulated by complex signaling pathways.

Purpose of the Study:

  • To identify and characterize a novel PTPase gene in fission yeast.
  • To investigate the role of this new PTPase, pyp2, in cell cycle regulation, particularly mitosis.
  • To elucidate the relationship between pyp2, the known PTPase pyp1, and other cell cycle regulators like cdc25 and wee1.

Main Methods:

  • Gene identification and cloning of the pyp2 gene.
  • Gene disruption and analysis of cell viability and cell cycle progression.
  • Complementation studies with existing mutants.
  • Analysis of protein sequence homology between pyp1 and pyp2.

Main Results:

  • A third PTPase gene, pyp2, was identified, encoding an 85 kDa protein.
  • pyp2 disruption alone had no effect, but was essential in pyp1-deficient strains.
  • Both pyp1 and pyp2 inhibit mitosis onset and rescue G2 arrest caused by cdc25 mutations.
  • pyp1 disruption advanced mitosis and suppressed wee1 overexpression, while pyp2 overexpression delayed mitosis via wee1.

Conclusions:

  • Fission yeast possesses at least two PTPases, pyp1 and pyp2, involved in mitotic control.
  • These PTPases function in opposition to the wee1 pathway, promoting mitotic entry.
  • Protein tyrosine phosphorylation plays a significant role in regulating the wee1 inhibitory pathway during mitosis.

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