More than folding: Localized functions of cytosolic chaperones

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

    Research output: Contribution to journalReview articlepeer-review

    308 Scopus citations


    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
    Issue number10
    StatePublished - Oct 2003

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology


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