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Nat Rev Mol Cell Biol. 2010 Aug;11(8):579-92. doi: 10.1038/nrm2941.

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

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  • 1Department of Cell Biology, University of Groningen, University Medical Center, 713 AV Groningen, The Netherlands. h.h.kampinga@med.umcg.nl

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  • Nat Rev Mol Cell Biol. 2010 Oct;11(10):750.

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.

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