When an Hsp70 protein is ATP bound, the lid is open and peptides bind and release relatively rapidly. When Hsp70 proteins are ADP bound, the lid is closed, and peptides are tightly bound to the substrate binding domain.

In this review, we focus on the mechanisms which regulate Hsp70 expression under ATP depletion, using ischaemia as a paradigmatic model for ATP depletion in vivo, and analyze the molecular targets for Hsp70-mediated protection against ATP depletion.

The ATPase cycle of Hsp70 consists of an alternation between the ATP state with low affinity and fast exchange rates for substrates, and the ADP state with high affinity and low exchange rates for substrates (fig. 2).

Jun 28, 2019 · J-domain protein (JDP)-mediated binding of substrate proteins to Hsp70·ATP, in conjunction with a direct JDP–Hsp70 interaction, synergistically triggers Hsp70 ATP hydrolysis and transition to...

In summary, this study provides structural evidence of robust ATP-dependent antiparallel dimerization of human inducible Hsp70 protein and suggests a novel role of TPR domain cochaperones in multichaperone complexes involving Hsp70 ATP-bound dimers.

Jan 3, 2023 · The assembly of the F1 domain and its linkage to the peripheral stalk is poorly understood. Here we show a dual function of the mitochondrial Hsp70 (mtHsp70) in the formation of the ATP...

Simplified flow chart of Hsp70 impact on ATP generation. High expression levels of Hsp70 in heat-shocked HeLa cells led to a shift in energy metabolism with increased anaerobic glycolysis and attenuated oxidative phosphorylation.

Feb 6, 1998 · ATP hydrolysis is the prime target for regulation, mainly by members of the DnaJ family (Liberek et al. 1991; McCarty et al. 1995), found in all Hsp70-containing compartments of prokaryotic and eukaryotic cells, as well as in several tumor viruses (Laufen et al. 1997).

Hsp70s bind ATP, and possess a weak ATPase activity. At the same time, Hsp70s recognize and bind short stretches of exposed polypeptide segments rich in hydrophobic residues in extended conformations that are normally found in unfolded or misfolded proteins.

Oct 14, 1993 · The molecular chaperone proteins, particularly Hsp60 and Hsp70, have been implicated in essential cell functions under both normal and stress conditions (reviewed in refs 1-5). Members of the family of heat-shock proteins of M(r) 70K, Hsp70, bind to unfolded proteins and short peptides.