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The HSP70 chaperone machinery: J proteins as drivers of functional specificity Kampinga HH; Craig EANat Rev Mol Cell Biol 2010[Aug]; 11 (8): 579-92Heat 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.|Adenosine Triphosphate/metabolism[MESH]|Guanine Nucleotide Exchange Factors/chemistry/metabolism[MESH]|HSP40 Heat-Shock Proteins/chemistry/*metabolism[MESH]|HSP70 Heat-Shock Proteins/chemistry/*metabolism[MESH]|Humans[MESH]|Models, Biological[MESH]|Models, Molecular[MESH]|Protein Binding[MESH]|Protein Folding[MESH]|Protein Interaction Domains and Motifs[MESH]|Saccharomyces cerevisiae Proteins/chemistry/metabolism[MESH] |
