Hsp70 Protein

Hsp70 proteins are central components of the cellular network of molecular chaperones. They assist in a wide range of processes, including the folding and assembly of newly synthesized proteins, refolding of misfolded and aggregated proteins, membrane translocation of organellar and secretory proteins, and control of the activity of regulatory proteins. The cellular levels of Hsp70 are thought to be at least partially regulated by the E3 ubiquitin ligase CHIP, which also targets a broad range of Hsp70 chaperone substrates for proteosomal degradation. Consistent with its diverse activities, genetic and biochemical studies have implicated Hsp70 in a range of diseases including cancer, neurodegeneration, allograft rejection and infection.

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