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The novel murine calmodulin-binding protein Sha1 disrupts mitotic spindle and replication checkpoint functions in

R Craig1, C Norbury

  • 1Imperial Cancer Research Fund, Molecular Oncology Laboratory, University of Oxford Institute of Molecular Medicine, John Radcliffe Hospital, Oxford OX3 9DS, UK.

Journal of Cell Science
|November 20, 1998
PubMed

Insights

Researchers identified a novel protein, Sha1, crucial for the S-M cell-cycle checkpoint. This protein regulates entry into mitosis and mitotic spindle functions, ensuring genomic integrity.

Area of Science:

  • Cell Biology
  • Genetics
  • Molecular Biology

Background:

  • The S-M checkpoint prevents cell division before DNA replication completion, maintaining genomic integrity.
  • Defects in this checkpoint lead to attempted mitosis with unreplicated chromosomes, causing the 'cut' phenotype in fission yeast.

Purpose of the Study:

  • To identify conserved molecules involved in the S-M checkpoint.
  • To investigate the function of novel proteins affecting cell cycle control and mitotic spindle integrity.

Main Methods:

  • Screening a murine cDNA library in Schizosaccharomyces pombe.
  • Inducing the 'cut' phenotype in hydroxyurea-arrested cells.
  • Analyzing the effects of a novel cDNA product (Sha1) on cell cycle progression and spindle function.
  • Investigating the role of calmodulin through overexpression studies.

Main Results:

  • A novel cDNA encoding a calmodulin-binding protein, Sha1, was identified.
  • Sha1 perturbs both the S-M checkpoint and mitotic spindle functions.
  • Overexpression of calmodulin suppressed the phenotypes induced by Sha1.
  • Sha1 is structurally related to Drosophila's abnormal spindle (asp) protein.

Conclusions:

  • Calmodulin-binding proteins are essential for coordinating mitotic spindle functions with mitotic entry.
  • These findings suggest conserved roles for calmodulin-binding proteins in cell cycle regulation across eukaryotes.

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