HSPB5 engages multiple states of a destabilized client to enhance chaperone activity in a stress-dependent manner.

ABSTRACT: Small heat shock proteins (sHSPs) delay protein aggregation in an ATP-independent manner by interacting with client proteins that are in states susceptible to aggregation, including destabilized states related to cellular stress. Up-regulation of sHSPs under stress conditions supports their critical role in cellular viability. Widespread distribution of sHSPs in most organisms implies conservation of function, but it remains unclear whether sHSPs implement common or distinct mechanisms to delay protein aggregation. Comparisons among various studies are confounded by the use of different model client proteins, different assays for both aggregation and sHSP/client interactions, and variable experimental conditions used to mimic cellular stress. To further define sHSP/client interactions and

SUBMITTER: Delbecq SP 

PROVIDER: S-EPMC6398148 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature