Cells must sense heat quickly to protect their proteins and membranes. Here, the authors show that membrane stretch detected by the membrane sensor Mid2 promotes rapid phosphorylation of the Hsp70 cha...

Heat shock protein 70 (Hsp70) is a molecular chaperone that plays a key role in cellular processes by assisting protein folding and preventing aggregation. During client-protein folding, Hsp70…

Evolutionary and mechanistic divergence in the Hsp70–Hsp110 chaperone system. Prokaryotic Hsp70s probably diversified into multiple orthologues that cooperated with co-chaperones such as JDPs and NEF...

Protein quality control (PQC) is carried out in part by the chaperone Hsp70 in concert with adapters of the J-domain protein (JDP) family. The JDPs, a…

Heat shock proteins 70 (HSP70) are highly conserved molecular chaperones found across all domains of life, where they play essential roles in cellular stress responses. While HSP70 homologs have been ...

Hsp70 chaperones facilitate protein folding, complex assembly and translocation through membranes. This Review discusses recent insights into how Hsp70 and its co-chaperones — J-domain proteins and nu...

Leder et al. show that the chaperones PDIA6, Hsp70 BiP, ERdj3, PDIA1 and Hsp90 form co-condensates within the endoplasmic reticulum, enhancing folding and preventing misfolding of client proteins.

Hsp70s use energy from ATP hydrolysis to unfold protein structures and solubilize stable aggregates and accumulate native species, even under adverse non-native conditions. To carry out its catalytic ...

Hsp70 and Hsp40 molecular chaperones form a central machinery that remodels client proteins involved in numerous biological processes. Here, we integr…

Abstract. Protein homeostasis relies on chaperones such as HSP70 and HSP90, which assist in the folding, activation, and turnover of client proteins. Their

Molecular chaperones play a central role in maintaining protein homeostasis. The highly conserved Hsp70 family of chaperones have major functions in folding of nascent peptides, protein refolding, and...

Hsp70s use energy from ATP hydrolysis to unfold protein structures and solubilize stable aggregates and accumulate native species, even under adverse non-native conditions. To carry out its catalytic ...

Zhang et al. describe computationally designed proteins that modulate Hsp70 ATPase activity. One of these designs refolds proteins, dissolves intracellular condensates, and uncovers their cellular rol...

The 70 kDa heat shock protein (Hsp70) chaperones control protein homeostasis in all ATP-containing cellular compartments. J-domain proteins (JDPs) coevolved with Hsp70s to trigger ATP hydrolysis and c...

The correct folding of proteins often requires the intervention molecular chaperones, which can occur co-translationally. Here the authors identify elements of yeast Ssb (Hsp70) that mediate ribosomal...

Nature Reviews Molecular Cell Biology, Published online: 27 October 2025; doi:10.1038/s41580-025-00890-9Hsp70 chaperones facilitate protein folding, complex assembly and translocation through membranes. This Review discusses recent insights into how Hsp70 and its co-chaperones — J-domain proteins and nucleotide exchange factors — exert such functions, achieve substrate specificity and determine protein fate (folding or degradation).