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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. One of the proteins that accumulate upon stress in yeast cells is Ola1p, know as the “super aggregator” Using a proximity labelling approach based upon the biotin ligase TurboID we were able to show that these Ola1p harbouring aggregates are, in fact, stress granules that interact with both mitochondria and LDs.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Peter Briza

LAB HEAD: Peter Briza

PROVIDER: PXD045513 | Pride | 2024-01-26

REPOSITORIES: Pride

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

Kovacs Melanie M Geltinger Florian F Schartel Lukas L Pöschl Simon S Briza Peter P Paschinger Manuel M Boros Kitti K Felder Thomas Klaus TK Wimmer Herbert H Duschl Jutta J Rinnerthaler Mark M

Journal of lipid research 20231109 12

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 tra ...[more]

PMID: 37949369

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