{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Heo JM"],"funding":["NIDDK NIH HHS","NIAMS NIH HHS","NIGMS NIH HHS"],"pagination":["465-80"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2998070"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["40(3)"],"pubmed_abstract":["We show that Ydr049 (renamed VCP/Cdc48-associated mitochondrial stress-responsive--Vms1), a member of an unstudied pan-eukaryotic protein family, translocates from the cytosol to mitochondria upon mitochondrial stress. Cells lacking Vms1 show progressive mitochondrial failure, hypersensitivity to oxidative stress, and decreased chronological life span. Both yeast and mammalian Vms1 stably interact with Cdc48/VCP/p97, a component of the ubiquitin/proteasome system with a well-defined role in endoplasmic reticulum-associated protein degradation (ERAD), wherein misfolded ER proteins are degraded in the cytosol. We show that oxidative stress triggers mitochondrial localization of Cdc48 and this is dependent on Vms1. When this system is impaired by mutation of Vms1, ubiquitin-dependent mitochon"],"journal":["Molecular cell"],"pubmed_title":["A stress-responsive system for mitochondrial protein degradation."],"pmcid":["PMC2998070"],"funding_grant_id":["R01 DK071962","R01 GM075061","R01 GM087346-03","K99 AR059190","R01 GM087346","GM087346","GM75061","DK071962","R56 DK071962","DK070149","R01 DK070149","R01 GM067945"],"pubmed_authors":["Rutter J","Ashrafi K","Heo JM","Livnat-Levanon N","Taylor EB","Jones KT","Ring J","Brodsky JL","Madeo F","Xie J","Gygi SP","Dephoure N","Glickman MH"],"additional_accession":[]},"is_claimable":false,"name":"A stress-responsive system for mitochondrial protein degradation.","description":"We show that Ydr049 (renamed VCP/Cdc48-associated mitochondrial stress-responsive--Vms1), a member of an unstudied pan-eukaryotic protein family, translocates from the cytosol to mitochondria upon mitochondrial stress. Cells lacking Vms1 show progressive mitochondrial failure, hypersensitivity to oxidative stress, and decreased chronological life span. Both yeast and mammalian Vms1 stably interact with Cdc48/VCP/p97, a component of the ubiquitin/proteasome system with a well-defined role in endoplasmic reticulum-associated protein degradation (ERAD), wherein misfolded ER proteins are degraded in the cytosol. We show that oxidative stress triggers mitochondrial localization of Cdc48 and this is dependent on Vms1. When this system is impaired by mutation of Vms1, ubiquitin-dependent mitochon","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Nov","modification":"2025-04-04T20:12:50.215Z","creation":"2019-03-27T00:37:13Z"},"accession":"S-EPMC2998070","cross_references":{"pubmed":["21070972"],"doi":["10.1016/j.molcel.2010.10.021"]}}