Ola1p trafficking indicates an interaction network between mitochondria, lipid droplets, and stress granules in times of stress.

ABSTRACT: Protein aggregates arise naturally under normal physiological conditions, but their formation is accelerated by age or stress-induced protein misfolding. When the stressful event dissolves, these aggregates are removed by mechanisms, such as aggrephagy, chaperone-mediated autophagy, refolding attempts, or the proteasome. It was recently shown that mitochondria in yeast cells may support these primarily cytosolic processes. Protein aggregates attach to mitochondria, and misfolded proteins are transported into the matrix and degraded by mitochondria-specific proteases. Using a proximity labeling method and colocalization with an established stress granule (SG) marker, we were able to show that these mitochondria-localized aggregates that harbor the "super aggregator" Ola1p are, in fact, SGs.

SUBMITTER: Kovacs M 

PROVIDER: S-EPMC10757043 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature