HSPB6: A lipid-dependent molecular chaperone inhibits α-synuclein aggregation.

ABSTRACT: The process of protein misfolding and aggregation is associated with various cytotoxic effects. Understanding how this phenomenon is regulated by the protein homeostasis system, however, is difficult, since it takes place through a complex non-linear network of coupled microscopic steps, including primary nucleation, fibril elongation, and secondary nucleation, which depend on environmental factors. To address this problem, we studied how the aggregation of α-synuclein, a protein associated with Parkinson's disease, is modulated by molecular chaperones and lipid membranes. We focused on small heat shock proteins (sHSPs/HSPBs), which interact with proteins and lipids and are upregulated during aging, a major risk factor for protein misfolding diseases. HSPBs act on different microscopic ste

SUBMITTER: Secco V 

PROVIDER: S-EPMC11402235 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature