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Life-span extension by a metacaspase in the yeast Saccharomyces cerevisiae

Journal article
Authors Sandra Malmgren Hill
Xinxin Hao
Beidong Liu
Thomas Nyström
Published in Science
Volume 344
Issue 6190
Pages 1389-1392
ISSN 0036-8075
Publication year 2014
Published at Department of Chemistry and Molecular Biology
Pages 1389-1392
Language en
Subject categories Cell Biology


Single-cell species harbor ancestral structural homologs of caspase proteases, although the evolutionary benefit of such apoptosis-related proteins in unicellular organisms is unclear. Here, we found that the yeast metacaspase Mca1 is recruited to the insoluble protein deposit (IPOD) and juxtanuclear quality-control compartment (JUNQ) during aging and proteostatic stress. Elevating MCA1 expression counteracted accumulation of unfolded proteins and aggregates and extended life span in a heat shock protein Hsp104 disaggregase- and proteasome-dependent manner. Consistent with a role in protein quality control, genetic interaction analysis revealed that MCA1 buffers against deficiencies in the Hsp40 chaperone YDJ1 in a caspase cysteine-dependent manner. Life-span extension and aggregate management by Mca1 was only partly dependent on its conserved catalytic cysteine, which suggests that Mca1 harbors both caspase-dependent and independent functions related to life-span control.

Page Manager: Webmaster|Last update: 9/11/2012

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