`The HSP70 chaperone machinery: J proteins as drivers of functional specificity

Harm H. Kampinga*, Elizabeth A. Craig

*Corresponding author for this work

    Research output: Contribution to journalReview articlepeer-review

    967 Citations (Scopus)

    Abstract

    Heat shock 70 kDa proteins (HSP70s) are ubiquitous molecular chaperones that function in a myriad of biological processes, modulating polypeptide folding, degradation and translocation across membranes, and protein-protein interactions. This multitude of roles is not easily reconciled with the universality of the activity of HSP70s in ATP-dependent client protein-binding and release cycles. Much of the functional diversity of the HSP70s is driven by a diverse class of cofactors: J proteins. Often, multiple J proteins function with a single HSP70. Some target HSP70 activity to clients at precise locations in cells and others bind client proteins directly, thereby delivering specific clients to HSP70 and directly determining their fate.

    Original languageEnglish
    Pages (from-to)579-592
    Number of pages14
    JournalNature Reviews Molecular Cell Biology
    Volume11
    Issue number8
    DOIs
    Publication statusPublished - Aug-2010

    Keywords

    • HEAT-SHOCK PROTEINS
    • NUCLEOTIDE EXCHANGE FACTOR
    • LAMBDA-DNA-REPLICATION
    • E3 UBIQUITIN LIGASE
    • ER-ASSOCIATED DEGRADATION
    • BULBAR MUSCULAR-ATROPHY
    • S CLUSTER BIOGENESIS
    • MOLECULAR CHAPERONES
    • ESCHERICHIA-COLI
    • SACCHAROMYCES-CEREVISIAE

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