Protein aggregates are associated with replicative aging without compromising protein quality control

Open access
Date
2015-11Type
- Journal Article
Citations
Cited 87 times in
Web of Science
Cited 89 times in
Scopus
ETH Bibliography
yes
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Abstract
Differentiation of cellular lineages is facilitated by asymmetric segregation of fate determinants between dividing cells. In budding yeast, various aging factors segregate to the aging (mother)-lineage, with poorly understood consequences. In this study, we show that yeast mother cells form a protein aggregate during early replicative aging that is maintained as a single, asymmetrically inherited deposit over the remaining lifespan. Surprisingly, deposit formation was not associated with stress or general decline in proteostasis. Rather, the deposit-containing cells displayed enhanced degradation of cytosolic proteasome substrates and unimpaired clearance of stress-induced protein aggregates. Deposit formation was dependent on Hsp42, which collected non-random client proteins of the Hsp104/Hsp70-refolding machinery, including the prion Sup35. Importantly, loss of Hsp42 resulted in symmetric inheritance of its constituents and prolonged the lifespan of the mother cell. Together, these data suggest that protein aggregation is an early aging-associated differentiation event in yeast, having a two-faceted role in organismal fitness. Show more
Permanent link
https://doi.org/10.3929/ethz-b-000107259Publication status
publishedExternal links
Journal / series
eLifeVolume
Pages / Article No.
Publisher
eLife Sciences PublicationsOrganisational unit
03532 - Barral, Yves / Barral, Yves
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Show all metadata
Citations
Cited 87 times in
Web of Science
Cited 89 times in
Scopus
ETH Bibliography
yes
Altmetrics