Multivalent protein-protein interactions are pivotal regulators of eukaryotic Hsp70 complexes.

ABSTRACT: Heat shock protein 70 (Hsp70) is a molecular chaperone and central regulator of protein homeostasis (proteostasis). Paramount to this role is Hsp70's binding to client proteins and co-chaperones to produce distinct complexes, such that understanding the protein-protein interactions (PPIs) of Hsp70 is foundational to describing its function and dysfunction in disease. Mounting evidence suggests that these PPIs include both "canonical" interactions, which are universally conserved, and "non-canonical" (or "secondary") contacts that seem to have emerged in eukaryotes. These two categories of interactions involve discrete binding surfaces, such that some clients and co-chaperones engage Hsp70 with at least two points of contact. While the contributions of canonical interactions to chaperone fu

SUBMITTER: Johnson OT 

PROVIDER: S-EPMC9346034 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature