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Molecular Chaperones

Volume 787 of the series Methods in Molecular Biology pp 33-44

Date:

Hsp90 and Client Protein Maturation

  • Natalie WayneAffiliated withDepartment of Biochemistry and Molecular Biology, University of Massachusetts Medical School
  • , Parul MishraAffiliated withDepartment of Biochemistry and Molecular Biology, University of Massachusetts Medical School
  • , Daniel N. BolonAffiliated withDepartment of Biochemistry and Molecular Biology, University of Massachusetts Medical School Email author 

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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