The Hsp70 chaperone machinery: J-proteins as drivers of functional specificity

By H. Kampinga, E. Craig. Nature reviews. Molecular cell biology, 2010

1,732 citations recorded by the source corpus.

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.

Subfields: Cell Biology, Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/b231398776de40397c93401665cceeb959785055

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Citations in the corpus

Pathways of cellular proteostasis in aging and disease (2018, background): “Proteins that are unable to fold through such Hsp70 cycles may be transferred to the chaperonin class of chaperones (Hsp60s), which includes GroEL/GroES in bacteria, Hsp60 in mitochondria, and TRiC/CCT in the eukaryotic cytosol (Fig.”
The Response to Heat Shock and Oxidative Stress in Saccharomyces cerevisiae (2012, background): “On the basis of the highly conserved J domain signature, 22 J proteins have been identified in S. cerevisiae (Kampinga and Craig 2010).”
In vivo aspects of protein folding and quality control (2016, background): “(74), amplifying the ability of Hsp70 to recognize a diverse range of clients.”
The heat shock response: life on the verge of death. (2010, positive): “J-domain-containing proteins (Kampinga and Craig, 2010).”
Molecular chaperones in protein folding and proteostasis (2011, background): “The ATP-dependent reaction cycle of HSP70 is regulated by chaperones of the HSP40 (also known as DnaJ) family and nucleotide-exchange factor”
Large-Scale Conformational Transitions and Dimerization Are Encoded in the Amino-Acid Sequences of Hsp70 Chaperones (2015, positive): “The Hsp70 cycle is further regulated by the cooperative action of co-chaperones: J-domain proteins (JDPs) strongly stimulate ATP-hydrolysis [16], whereas nucleotide exchange factors (NEFs) catalyse the release of ADP [17,18].”