Journal article
Hsp90 and co-chaperones twist the functions of diverse client proteins
Biopolymers, Vol.93(3), pp.211-217
03/2010
Handle:
https://hdl.handle.net/2376/102639
PMCID: PMC2810645
PMID: 19697319
Abstract
Hsp90 molecular chaperones are required for the stability and activity of a diverse range of client proteins that have critical roles in signal transduction, cellular trafficking, chromatin remodeling, cell growth, differentiation, and reproduction. Mammalian cells contain three types of Hsp90s: cytosolic Hsp90, mitochondrial Trap-1, and Grp94 of the endoplasmic reticulum. Each of the Hsp90s, as well as the bacterial homolog, HtpG, hydrolyze ATP and undergo similar conformational changes. Unlike the other forms of Hsp90, cytosolic Hsp90 function is dependent on a battery of co-chaperone proteins that regulate the ATPase activity of Hsp90 or direct Hsp90 to interact with specific client proteins. This review will summarize what is known about Hsp90's ability to mediate the folding and activation of diverse client proteins that contribute to human diseases, such as cancer and fungal and viral infections.
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Details
- Title
- Hsp90 and co-chaperones twist the functions of diverse client proteins
- Creators
- Abbey Zuehlke - Department of Microbiology, Molecular Biology and Biochemistry and the Center for Reproductive Biology, University of Idaho, Moscow, ID 83844-3052, USAJill L Johnson
- Publication Details
- Biopolymers, Vol.93(3), pp.211-217
- Academic Unit
- UNKNOWN
- Publisher
- United States
- Grant note
- P20 RR015587 / NCRR NIH HHS P20 RR015587-105898 / NCRR NIH HHS
- Identifiers
- 99900546632001842
- Language
- English
- Resource Type
- Journal article