The Cdc48-Vms1 complex maintains 26S proteasome architecture.
Identifieur interne : 000F54 ( Main/Merge ); précédent : 000F53; suivant : 000F55The Cdc48-Vms1 complex maintains 26S proteasome architecture.
Auteurs : Joseph R. Tran ; Jeffrey L. Brodsky [États-Unis]Source :
- The Biochemical journal [ 1470-8728 ] ; 2014.
Descripteurs français
- KwdFr :
- Adenosine triphosphatases (métabolisme), Proteasome endopeptidase complex (métabolisme), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines de transport (génétique), Protéines de transport (métabolisme), Protéines du cycle cellulaire (métabolisme), Protéines ubiquitinées (métabolisme), Saccharomyces cerevisiae (cytologie), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme).
- MESH :
- cytologie : Saccharomyces cerevisiae.
- génétique : Protéines de Saccharomyces cerevisiae, Protéines de transport, Saccharomyces cerevisiae.
- métabolisme : Adenosine triphosphatases, Proteasome endopeptidase complex, Protéines de Saccharomyces cerevisiae, Protéines de transport, Protéines du cycle cellulaire, Protéines ubiquitinées, Saccharomyces cerevisiae.
English descriptors
- KwdEn :
- Adenosine Triphosphatases (metabolism), Carrier Proteins (genetics), Carrier Proteins (metabolism), Cell Cycle Proteins (metabolism), Proteasome Endopeptidase Complex (metabolism), Saccharomyces cerevisiae (cytology), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Ubiquitinated Proteins (metabolism).
- MESH :
- chemical , genetics : Carrier Proteins, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Adenosine Triphosphatases, Carrier Proteins, Cell Cycle Proteins, Proteasome Endopeptidase Complex, Saccharomyces cerevisiae Proteins, Ubiquitinated Proteins.
- cytology : Saccharomyces cerevisiae.
- genetics : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
Abstract
The 26S proteasome is responsible for most regulated protein turnover and for the degradation of aberrant proteins in eukaryotes. The assembly of this ~2.5 MDa multicatalytic protease requires several dedicated chaperones and, once assembled, substrate selectivity is mediated by ubiquitin conjugation. After modification with ubiquitin, substrates are escorted to the proteasome by myriad factors, including Cdc48 (cell-division cycle 48). Cdc48 also associates with numerous cofactors, but, to date, it is unclear whether each cofactor facilitates proteasome delivery. We discovered that yeast lacking a conserved Cdc48 cofactor, Vms1 [VCP (valosin-containing protein)/Cdc48-associated mitochondrial stress-responsive], accumulate proteasome-targeted ubiquitinated proteins. Vms1 mutant cells also contain elevated levels of unassembled 20S proteasome core particles and select 19S cap subunits. In addition, we found that the ability of Vms1 to support 26S proteasome assembly requires Cdc48 interaction, and that the loss of Vms1 reduced 26S proteasome levels and cell viability after prolonged culture in the stationary phase. The results of the present study highlight an unexpected link between the Cdc48-Vms1 complex and the preservation of proteasome architecture, and indicate how perturbed proteasome assembly affects the turnover of ubiquitinated proteins and maintains viability in aging cells.
DOI: 10.1042/BJ20131161
PubMed: 24351022
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pubmed:24351022Le document en format XML
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Tran</name></author><author><name sortKey="Brodsky, Jeffrey L" sort="Brodsky, Jeffrey L" uniqKey="Brodsky J" first="Jeffrey L" last="Brodsky">Jeffrey L. Brodsky</name><affiliation wicri:level="4"><nlm:affiliation>*Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, U.S.A.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>*Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260</wicri:regionArea><placeName><region type="state">Pennsylvanie</region><settlement type="city">Pittsburgh</settlement></placeName><orgName type="university">Université de Pittsburgh</orgName></affiliation></author></analytic><series><title level="j">The Biochemical journal</title><idno type="eISSN">1470-8728</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adenosine Triphosphatases (metabolism)</term><term>Carrier Proteins (genetics)</term><term>Carrier Proteins (metabolism)</term><term>Cell Cycle Proteins (metabolism)</term><term>Proteasome Endopeptidase Complex (metabolism)</term><term>Saccharomyces cerevisiae (cytology)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (genetics)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>Ubiquitinated Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Adenosine triphosphatases (métabolisme)</term><term>Proteasome endopeptidase complex (métabolisme)</term><term>Protéines de Saccharomyces cerevisiae (génétique)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Protéines de transport (génétique)</term><term>Protéines de transport (métabolisme)</term><term>Protéines du cycle cellulaire (métabolisme)</term><term>Protéines ubiquitinées (métabolisme)</term><term>Saccharomyces cerevisiae (cytologie)</term><term>Saccharomyces cerevisiae (génétique)</term><term>Saccharomyces cerevisiae (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Carrier Proteins</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Adenosine Triphosphatases</term><term>Carrier Proteins</term><term>Cell Cycle Proteins</term><term>Proteasome Endopeptidase Complex</term><term>Saccharomyces cerevisiae Proteins</term><term>Ubiquitinated Proteins</term></keywords><keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines de transport</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Adenosine triphosphatases</term><term>Proteasome endopeptidase complex</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines de transport</term><term>Protéines du cycle cellulaire</term><term>Protéines ubiquitinées</term><term>Saccharomyces cerevisiae</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The 26S proteasome is responsible for most regulated protein turnover and for the degradation of aberrant proteins in eukaryotes. The assembly of this ~2.5 MDa multicatalytic protease requires several dedicated chaperones and, once assembled, substrate selectivity is mediated by ubiquitin conjugation. After modification with ubiquitin, substrates are escorted to the proteasome by myriad factors, including Cdc48 (cell-division cycle 48). Cdc48 also associates with numerous cofactors, but, to date, it is unclear whether each cofactor facilitates proteasome delivery. We discovered that yeast lacking a conserved Cdc48 cofactor, Vms1 [VCP (valosin-containing protein)/Cdc48-associated mitochondrial stress-responsive], accumulate proteasome-targeted ubiquitinated proteins. Vms1 mutant cells also contain elevated levels of unassembled 20S proteasome core particles and select 19S cap subunits. In addition, we found that the ability of Vms1 to support 26S proteasome assembly requires Cdc48 interaction, and that the loss of Vms1 reduced 26S proteasome levels and cell viability after prolonged culture in the stationary phase. The results of the present study highlight an unexpected link between the Cdc48-Vms1 complex and the preservation of proteasome architecture, and indicate how perturbed proteasome assembly affects the turnover of ubiquitinated proteins and maintains viability in aging cells.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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