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Related Experiment Videos

Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent

D F Smith1, L Whitesell, S C Nair

  • 1Department of Pharmacology, University of Nebraska Medical Center, Omaha 68198, USA.

Molecular and Cellular Biology
|December 1, 1995
PubMed
Summary

Geldanamycin (GA) halts progesterone receptor (PR) assembly by blocking p23 binding to hsp90. This prevents PR from binding progesterone, impacting its function both in vitro and in intact cells.

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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • Progesterone receptor (PR) assembly involves complex interactions among at least eight molecular chaperone proteins.
  • Understanding PR assembly is crucial for comprehending its cellular function and regulation.

Purpose of the Study:

  • To investigate the role of molecular chaperones, specifically hsp90, in progesterone receptor (PR) heterocomplex assembly.
  • To elucidate the mechanism by which geldanamycin (GA) affects PR assembly and function.

Main Methods:

  • In vitro assembly of PR heterocomplexes using molecular chaperone components.
  • Utilizing geldanamycin (GA), an hsp90 binding agent, to arrest PR assembly at intermediate stages.
  • Analysis of the composition of intermediate and mature PR complexes using biochemical assays.

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  • Assessment of PR hormone-binding capacity in vitro and in intact cells.

    • Main Results:

    • Geldanamycin (GA) treatment arrests PR assembly at an intermediate step characterized by the presence of hsp70, p60, and p48, and the absence of immunophilins and p23.
    • GA-mediated arrest is attributed to the inhibition of p23 binding to hsp90.
    • Arrested PR complexes fail to bind progesterone, despite containing hsp90.
    • GA rapidly blocks PR hormone-binding capacity in intact cells and alters PR complex composition similarly to in vitro findings.

    Conclusions:

    • Geldanamycin (GA) provides a tool to dissect the ordered pathway of progesterone receptor (PR) assembly.
    • The study presents an updated model for the cyclic assembly pathway of PR complexes.
    • GA's ability to inhibit PR function in cells highlights the importance of chaperone-mediated assembly for receptor activity.