Impact of N-terminal domain on the sHSP Lo18 function.

ABSTRACT: External stress conditions can induce disturbances in the internal environment of cells, sufficient for protein misfolding or membrane disorganization. To cope with this phenomenon, cells have developed several strategies, including the production of heat stress proteins (HSPs). These include small heat shock proteins (sHSPs). sHSPs share a characteristic three-dimensional architecture, with a central α-crystalline domain (ACD) flanked by two terminal domains. This structural organization enables them to form a variety of oligomeric complexes, giving these proteins their function. As large oligomers, all sHSPs act as chaperones. Conversely, some of them adopt a lipochaperone role when present in dimeric form. While the role of the ACD domain in oligomerization and the mechanism of action o

SUBMITTER: Bellanger T 

PROVIDER: S-EPMC12830648 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature