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Trends Biochem Sci. 2003 Oct;28(10):541-7.

More than folding: localized functions of cytosolic chaperones.

Author information

1
Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18a, D-82152, Martinsried, Germany. young@biochem.mpg.de

Abstract

Compared with other chaperone systems, heat shock proteins Hsp70 and Hsp90 interact with a larger variety of co-chaperone proteins that regulate their activity or aid in the folding of specific substrate proteins. Although many co-chaperones are soluble cytosolic proteins, co-chaperone domains are also found in modular adaptor proteins, which are often localized to intracellular membranes or elements of the cytoskeleton. These specialized co-chaperones include auxilin, cysteine string protein, Tom70, UNC-45 and homologs of Bag-1. The localized co-chaperones can harness the ATP-dependent mechanisms of Hsp70 and Hsp90 to do conformational work in diverse functional contexts, including vesicle secretion and recycling, protein transport and the regulated assembly and/or disassembly of protein complexes. Such flexibility is unique to the cytosolic Hsp70 and Hsp90 chaperone system.

PMID:
14559183
DOI:
10.1016/j.tibs.2003.08.009
[Indexed for MEDLINE]

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