HSC70 Heat-Shock Proteins

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  Subject Areas on Research

  • A bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteins. 
  • Changes in protein function underlie the disease spectrum in patients with CHIP mutations. 
  • Human erythrocyte clathrin and clathrin-uncoating protein. 
  • Proteomic identification and functional characterization of MYH9, Hsc70, and DNAJA1 as novel substrates of HDAC6 deacetylase activity. 
  • Purinergic receptor X7 is a key modulator of metabolic oxidative stress-mediated autophagy and inflammation in experimental nonalcoholic steatohepatitis. 
  • Selective externalization of an ATP-binding protein structurally related to the clathrin-uncoating ATPase/heat shock protein in vesicles containing terminal transferrin receptors during reticulocyte maturation. 
  • The 70-kDa heat shock cognate protein (Hsc73) gene is enhanced by ovarian hormones in the ventromedial hypothalamus. 
  • The E3 ubiquitin ligase CHIP and the molecular chaperone Hsc70 form a dynamic, tethered complex.