Metacaspase Yca1 is required for clearance of insoluble protein aggregates

In complex organisms, caspase proteases mediate a variety of cell behaviors, including proliferation, differentiation, and programmed cell death/apoptosis. Structural homologs to the caspase family (termed metacaspases) engage apoptosis in single-cell eukaryotes, yet the molecular mechanisms that co...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2010-07, Vol.107 (30), p.13348-13353
Main Authors: Lee, Robin E. C., Brunette, Steve, Puente, Lawrence G., Megeney, Lynn A., Olson, Eric N.
Format: Article
Language:English
Subjects:
Apoptosis
Biological Sciences
Carrier Proteins - genetics
Carrier Proteins - metabolism
Caspases - genetics
Caspases - metabolism
Cell aggregates
Cell cycle
Cell growth
Cytosol - metabolism
Enzyme kinetics
Green Fluorescent Proteins - genetics
Green Fluorescent Proteins - metabolism
Heat stress disorders
Heat-Shock Proteins - genetics
Heat-Shock Proteins - metabolism
Immunoblotting
Models, Biological
Molecular Chaperones - genetics
Molecular Chaperones - metabolism
Mother cells
Mutation
Oxidative stress
Prions
Protein Binding
Proteins
Proteome - genetics
Proteome - metabolism
Proteomics
Proteomics - methods
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
Vacuoles - metabolism
Yeast
Yeasts
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Summary:In complex organisms, caspase proteases mediate a variety of cell behaviors, including proliferation, differentiation, and programmed cell death/apoptosis. Structural homologs to the caspase family (termed metacaspases) engage apoptosis in single-cell eukaryotes, yet the molecular mechanisms that contribute to nondeath roles are currently undefined. Here, we report an unexpected role for the Saccharomyces cerevisiae metacaspase Yca1 in protein quality control. Quantitative proteomic analysis of Δyca1 cells identified significant alterations to vacuolar catabolism and stress-response proteins in the absence of induced stress. Yca1 protein complexes are enriched for aggregate-remodeling chaperones that colocalize with Yca1-GFP fusions. Finally, deletion and inactivation mutants of Yca1 accrue protein aggregates and autophagic bodies during log-phase growth. Together, our results show that Yca1 contributes to the fitness and adaptability of growing yeast through an aggregate remodeling activity.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.1006610107