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Methods Mol Biol. 2018;1709:397-422. doi: 10.1007/978-1-4939-7477-1_28.

Evidence for Hsp90 Co-chaperones in Regulating Hsp90 Function and Promoting Client Protein Folding.

Author information

1
Department of Biological Sciences, University of Texas at El Paso and the Border Biomedical Research Center, El Paso, TX, 79968, USA.
2
Department of Biological Sciences and the Center for Reproductive Biology, University of Idaho, Moscow, ID, 83844-3051, USA. jilljohn@uidaho.edu.

Abstract

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. 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.

KEYWORDS:

Co-chaperones; Hop; Hsp90; Immunophilins; p23

PMID:
29177674
DOI:
10.1007/978-1-4939-7477-1_28
[Indexed for MEDLINE]

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