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

作者：Kampinga Harm H^*; Craig Elizabeth A

来源：Nature Reviews Molecular Cell Biology, 2010, 11(8): 579-592.

DOI：10.1038/nrm2941

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.

• 出版日期2010-8