期刊
BIOPOLYMERS
卷 93, 期 3, 页码 211-217出版社
WILEY
DOI: 10.1002/bip.21292
关键词
molecular machines; protein folding; molecular chaperones
资金
- National Center for Research Resources (NCRR)
- National Institutes of Health (NIH) [P20 RR015587]
- National Science Foundation [MCB-0744522]
- NATIONAL CENTER FOR RESEARCH RESOURCES [P20RR015587] Funding Source: NIH RePORTER
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, chromatinf 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. (C) 2009 Wiley Periodicals, Inc. Biopolymers 93: 211-217, 2010.
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