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Asymmetric Inheritance of Aggregated Proteins and Age Reset in Yeast Are Regulated by Vac17-Dependent Vacuolar Functions

Journal article
Authors Sandra Malmgren Hill
Xinxin Hao
Johan Grönvall
Stephanie Spikings-Nordby
Per O Widlund
T. Amen
Anna Jorhov
Rebecca Josefson
D. Kaganovich
Beidong Liu
Thomas Nyström
Published in Cell Reports
Volume 16
Issue 3
Pages 826-838
ISSN 2211-1247
Publication year 2016
Published at Institute of Biomedicine
Department of Chemistry and Molecular Biology
Pages 826-838
Language en
Links dx.doi.org/10.1016/j.celrep.2016.06...
Keywords life-span, saccharomyces-cerevisiae, damaged proteins, misfolded, proteins, actin cytoskeleton, quality-control, budding yeast, v-atpase, fusion, chaperone, Cell Biology
Subject categories Cell and Molecular Biology

Abstract

Age can be reset during mitosis in both yeast and stem cells to generate a young daughter cell from an aged and deteriorated one. This phenomenon requires asymmetry-generating genes (AGGs) that govern the asymmetrical inheritance of aggregated proteins. Using a genome-wide imaging screen to identify AGGs in Saccharomyces cerevisiae, we discovered a previously unknown role for endocytosis, vacuole fusion, and the myosin-dependent adaptor protein Vac17 in asymmetrical inheritance of misfolded proteins. Overproduction of Vac17 increases deposition of aggregates into cytoprotective vacuole-associated sites, counteracts age-related breakdown of endocytosis and vacuole integrity, and extends replicative lifespan. The link between damage asymmetry and vesicle trafficking can be explained by a direct interaction between aggregates and vesicles. We also show that the protein disaggregase Hsp104 interacts physically with endocytic vesicle-associated proteins, such as the dynamin-like protein, Vps1, which was also shown to be required for Vac17-dependent sequestration of protein aggregates. These data demonstrate that two physiognomies of aging-reduced endocytosis and protein aggregation-are interconnected and regulated by Vac17.

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