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Related Experiment Videos

The 14-3-3 proteins positively regulate rapamycin-sensitive signaling

P G Bertram1, C Zeng, J Thorson

  • 1Department of Pathology Washington University School of Medicine St. Louis, Missouri, 63110, USA.

Current Biology : CB
|November 21, 1998
PubMed
Summary

Researchers identified 14-3-3 proteins as key players in Tor signaling, a pathway targeted by the immunosuppressant rapamycin. Understanding 14-3-3 protein function is crucial for rapamycin-sensitive signaling.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The kinase Tor is a critical regulator of cell cycle progression and a target of the immunosuppressive drug rapamycin.
  • The precise molecular mechanisms underlying Tor signaling pathways remain largely unknown.

Purpose of the Study:

  • To investigate the role of 14-3-3 proteins in rapamycin-sensitive signaling pathways.
  • To elucidate the structural and functional aspects of 14-3-3 proteins in yeast.

Main Methods:

  • Isolation of Saccharomyces cerevisiae genes BMH1 and BMH2 as multicopy suppressors of rapamycin-induced growth inhibition.
  • Analysis of the effects of BMH gene deletions and mutations in the 14-3-3 phosphopeptide-binding pocket on rapamycin sensitivity.

Main Results:

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  • BMH1 and BMH2, encoding 14-3-3 homologs, were identified as suppressors of rapamycin's growth-inhibitory effects.
  • Gene dosage of BMH genes influenced hypersensitivity to rapamycin.
  • Mutations affecting phosphoserine-binding abolished rapamycin resistance, while substitutions near these sites conferred dominant resistance.

Conclusions:

  • 14-3-3 proteins are integral components of rapamycin-sensitive signaling pathways.
  • The study provides novel insights into the structure-function relationships of 14-3-3 proteins, particularly their role in phosphopeptide binding and signaling modulation.