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Related Experiment Videos

A cyclophilin function in Hsp90-dependent signal transduction

A A Duina1, H C Chang, J A Marsh

  • 1Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, 2153 Sheridan Road, Evanston, IL 60208, USA.

Science (New York, N.Y.)
|December 6, 1996
PubMed
Summary

Cyclophilins (CyP-40) in yeast interact with Hsp90 chaperone. Deleting CPR7 caused growth defects and impaired Hsp90-dependent signaling, suggesting a general role for CyP-40 cyclophilins in these pathways.

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Area of Science:

  • Molecular biology
  • Cellular signaling
  • Protein biochemistry

Background:

  • Cyclophilin-40 (CyP-40) homologs, Cpr6 and Cpr7, are present in Saccharomyces cerevisiae.
  • Hsp90 is a crucial protein chaperone involved in various signal transduction pathways.
  • Sti1 is another known component of the Hsp90 chaperone machinery.

Purpose of the Study:

  • To investigate the interaction between yeast CyP-40 homologs (Cpr6, Cpr7) and Hsp90.
  • To determine the functional significance of this interaction in yeast.
  • To assess the role of CyP-40 cyclophilins in Hsp90-dependent signal transduction.

Main Methods:

  • Yeast genetics: construction of deletion mutants for CPR7.
  • Analysis of protein complexes involving Cpr6, Cpr7, and Hsp90.

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  • Phenotypic analysis of yeast strains under various stress conditions.
  • Assay of Hsp90-dependent signaling pathways (glucocorticoid receptor, pp60(v-src) kinase activity).

    • Main Results:

    • Cpr6 and Cpr7 form complexes with Hsp90 in yeast.
    • Deletion of CPR7 resulted in severe growth defects when Hsp90 or Sti1 levels were reduced.
    • Null mutations in CPR7 negatively impacted the activity of heterologous Hsp90-dependent signal transducers.

    Conclusions:

    • Yeast CyP-40 cyclophilins (Cpr6, Cpr7) associate with the Hsp90 chaperone complex.
    • These cyclophilins are important for maintaining cellular growth and Hsp90 function, particularly under stress.
    • CyP-40 cyclophilins play a general role in Hsp90-dependent signal transduction pathways in yeast.