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- Title
The HSP70 chaperone machinery: J proteins as drivers of functional specificity.
- Authors
Kampinga, Harm H; Craig, Elizabeth A
- 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.
- Publication
Nature reviews. Molecular cell biology, 2010, Vol 11, Issue 8, p579
- ISSN
1471-0080
- Publication type
Journal Article
- DOI
10.1038/nrm2941