Book chapter
The Role of p23, Hop, Immunophilins, and Other Co-chaperones in Regulating Hsp90 Function
Molecular Chaperones, pp.45-66
Methods in Molecular Biology, Humana Press
08/08/2011
Handle:
https://hdl.handle.net/2376/105280
PMID: 21898226
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 (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.
Metrics
5 Record Views
Details
- Title
- The Role of p23, Hop, Immunophilins, and Other Co-chaperones in Regulating Hsp90 Function
- Creators
- Marc B Cox - Border Biomedical Research Center, El Paso, USAJill L Johnson - Department of Microbiology, Molecular Biology, and Biochemistry, University of Idaho, Moscow, USA
- Publication Details
- Molecular Chaperones, pp.45-66
- Academic Unit
- UNKNOWN
- Series
- Methods in Molecular Biology
- Publisher
- Humana Press; Totowa, NJ
- Identifiers
- 99900546936401842
- Language
- English
- Resource Type
- Book chapter