Human Small Heat Shock Protein B8 Inhibits Protein Aggregation without Affecting the Native Folding Process.

ABSTRACT: Small Heat Shock Proteins (sHSPs) are key components of our Protein Quality Control system and are thought to act as reservoirs that neutralize irreversible protein aggregation. Yet, sHSPs can also act as sequestrases, promoting protein sequestration into aggregates, thus challenging our understanding of their exact mechanisms of action. Here, we employ optical tweezers to explore the mechanisms of action of the human small heat shock protein HSPB8 and its pathogenic mutant K141E, which is associated with neuromuscular disease. Through single-molecule manipulation experiments, we studied how HSPB8 and its K141E mutant affect the refolding and aggregation processes of the maltose binding protein. Our data show that HSPB8 selectively suppresses protein aggregation without affecting the nativ

SUBMITTER: Choudhary D 

PROVIDER: S-EPMC10360156 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature