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Related Experiment Videos

Cyclophilin-40: evidence for a dimeric complex with hsp90

K Hoffmann1, R E Handschumacher

  • 1Department of Pharmacology, Yale University School of Medicine, New Haven, CT 06520, USA.

The Biochemical Journal
|April 1, 1995
PubMed
Summary

Human cyclophilin 40 (CyP-40) primarily associates with heat-shock protein 90 (hsp90), forming complexes that may aid in protein folding and trafficking. This interaction is independent of cyclosporin A and heat-shock protein 70.

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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • Cyclophilin 40 (CyP-40) is a ubiquitous protein involved in cellular processes.
  • Heat-shock proteins, such as hsp90, are known chaperones involved in protein folding and stability.

Purpose of the Study:

  • To identify cellular components associated with human cyclophilin 40 (CyP-40).
  • To investigate the relationship between CyP-40 and heat-shock proteins.

Main Methods:

  • Expression of human CyP-40 as a glutathione S-transferase (GST) fusion protein.
  • Utilized a GSH affinity matrix to isolate interacting proteins from tissue extracts.
  • Analyzed protein associations using various biochemical techniques.

Main Results:

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  • Heat-shock protein 90 (hsp90) was identified as the predominant protein associated with CyP-40.
  • The CyP-40-hsp90 complex exists in significant concentrations in various tissues.
  • Association with hsp90 was independent of heat-shock protein 70 and cyclosporin A (CsA).
  • The hsp90 binding site on CyP-40 was mapped to its C-terminal region, distinct from its isomerase and CsA binding activities.

Conclusions:

  • CyP-40 and hsp90 form a stable, biologically relevant complex in many tissues.
  • This association suggests a potential shared role in protein folding and cellular trafficking.
  • The functional domains of CyP-40 can be functionally separated regarding hsp90 binding and isomerase activity.