More than folding

Localized functions of cytosolic chaperones

Jason C. Young, José M. Barral, F. Ulrich Hartl

Research output: Contribution to journalArticle

282 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)541-547
Number of pages7
JournalTrends in Biochemical Sciences
Volume28
Issue number10
DOIs
StatePublished - Oct 2003
Externally publishedYes

Fingerprint

Proteins
Auxilins
Intracellular Membranes
Recycling
Protein Transport
Heat-Shock Proteins
Cytoskeleton
Adenosine Triphosphate
Membranes
Substrates
cysteine string protein

ASJC Scopus subject areas

  • Biochemistry

Cite this

More than folding : Localized functions of cytosolic chaperones. / Young, Jason C.; Barral, José M.; Hartl, F. Ulrich.

In: Trends in Biochemical Sciences, Vol. 28, No. 10, 10.2003, p. 541-547.

Research output: Contribution to journalArticle

Young, Jason C. ; Barral, José M. ; Hartl, F. Ulrich. / More than folding : Localized functions of cytosolic chaperones. In: Trends in Biochemical Sciences. 2003 ; Vol. 28, No. 10. pp. 541-547.
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