Molecular Chaperones pp 33-44

Part of the Methods in Molecular Biology book series (MIMB, volume 787)

Hsp90 and Client Protein Maturation

Protocol

Abstract

Heat-shock protein 90 (Hsp90) is a molecular chaperone that assists in the maturation of a limited set of substrate proteins that are collectively referred to as clients. The majority of identified Hsp90 clients are involved in signal transduction, including many steroid hormone receptors and kinases. A handful of Hsp90 clients can be classified as nonsignal transduction proteins, including telomerase, cystic fibrosis transmembrane conductance regulator, and antigenic peptides destined for major histocompatibility complex. Because Hsp90 clients are causative agents in cancer and cystic fibrosis, research on Hsp90 has intensified in recent years. We review the historical path of Hsp90 research within each class of client (kinase, hormone receptor, and nonsignal transduction clients) and highlight current areas of active investigation.

Key words

Hsp90 Chaperone ATPase Kinase Steroid hormone receptor Signal transduction Telomerase CFTR Antigen presentation 

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© Springer Science+Business Media, LLC 2011

Authors and Affiliations

  1. 1.Department of Biochemistry and Molecular BiologyUniversity of Massachusetts Medical SchoolWorcesterUSA

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