Molecular Chaperones

Volume 787 of the series Methods in Molecular Biology pp 45-66


The Role of p23, Hop, Immunophilins, and Other Co-chaperones in Regulating Hsp90 Function

  • Marc B. CoxAffiliated withDepartment of Biological Sciences, University of Texas at El PasoBorder Biomedical Research Center
  • , Jill L. JohnsonAffiliated withDepartment of Microbiology, Molecular Biology, and Biochemistry, University of Idaho Email author 

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Molecular chaperones are a diverse group of highly conserved proteins that transiently interact with partially folded polypeptide chains during normal cellular processes, such as protein translation, translocation, and disassembly of protein complexes (1). Prior to folding or after denaturation, hydrophobic residues that are normally sequestered within a folded protein are exposed to the aqueous environment and are prone to aggregation or misfolding. Multiple classes of molecular chaperones, such as Hsp70s and Hsp40s, recognize and transiently bind polypeptides with exposed hydrophobic stretches in order to prevent misfolding. Other types of chaperones, such as Hsp90, have more specialized functions in that they appear to interact with only a subset of cellular proteins. This chapter focuses on the role of Hsp90 and partner co-chaperones in promoting the folding and activation of a diverse group of proteins with critical roles in cellular signaling and function.

Key words

Hsp90 p23 Co-chaperone Immunophilin Protein folding