Heat shock protein 70 family (Hsp70)

The heat shock protein 70 family (Hsp70) comprises a group of highly conserved molecular chaperones of approximately 70 kDa that play a central role in the maintenance of protein homeostasis (proteostasis) in all cells[1][2][4][5]. Hsp70s assist in the folding of newly synthesized proteins, refolding misfolded or denatured proteins, preventing protein aggregation under stress, and targeting damaged proteins for degradation[1][2][4]. They operate through an ATP-dependent mechanism; the protein has an N-terminal ATPase domain, a substrate binding domain that recognizes hydrophobic peptide segments, and a C-terminal domain acting as a lid over the binding site[1][7]. Hsp70 family members are induced by cellular stress (heat, oxidative stress, toxins), and their overexpression is commonly observed in cancer, where they protect tumor cells from apoptosis and environmental insults[4][5]. Hsp70s are increasingly recognized as important therapeutic targets, particularly in oncology and neurodegeneration, due to their essential role in cell survival, protein quality control, and cellular stress adaptation[4][5].

Other names

70 kDa heat shock proteinsHsp70 familyHsp70sHSP70 Heat-Shock ProteinsHsp70 chaperones

ATPase inhibition (stabilizes ADP-bound form, blocks chaperone cycle); Disruption of substrate binding; Promotion of protein degradation or aggregation in cancer cells; Induction of apoptotic pathways via stress overload in tumor cells