Reversible 26S proteasome disassembly upon mitochondrial stress.
Identifieur interne : 003544 ( Main/Curation ); précédent : 003543; suivant : 003545Reversible 26S proteasome disassembly upon mitochondrial stress.
Auteurs : Nurit Livnat-Levanon [Israël] ; Éva Kevei [Allemagne] ; Oded Kleifeld [Australie] ; Daria Krutauz [Israël] ; Alexandra Segref [Allemagne] ; Teresa Rinaldi [Italie] ; Zoi Erpapazoglou [France] ; Mickael Cohen [France] ; Noa Reis [Israël] ; Thorsten Hoppe [Allemagne] ; Michael H. Glickman [Israël]Source :
- Cell reports [ 2211-1247 ] ; 2014.
Descripteurs français
- KwdFr :
- Animaux, Antioxydants (pharmacologie), Caenorhabditis elegans (métabolisme), Cricetinae, Cystéine (métabolisme), Espèces réactives de l'oxygène (métabolisme), Lignée cellulaire, Mitochondries (), Mitochondries (métabolisme), Multimérisation de protéines, Proteasome endopeptidase complex (métabolisme), Saccharomyces cerevisiae (métabolisme), Stress oxydatif, Ubiquitine (métabolisme).
- MESH :
English descriptors
- KwdEn :
- Animals, Antioxidants (pharmacology), Caenorhabditis elegans (metabolism), Cell Line, Cricetinae, Cysteine (metabolism), Mitochondria (drug effects), Mitochondria (metabolism), Oxidative Stress, Proteasome Endopeptidase Complex (metabolism), Protein Multimerization, Reactive Oxygen Species (metabolism), Saccharomyces cerevisiae (metabolism), Ubiquitin (metabolism).
- MESH :
- chemical , metabolism : Cysteine, Proteasome Endopeptidase Complex, Reactive Oxygen Species, Ubiquitin.
- chemical , pharmacology : Antioxidants.
- drug effects : Mitochondria.
- metabolism : Caenorhabditis elegans, Mitochondria, Saccharomyces cerevisiae.
- Animals, Cell Line, Cricetinae, Oxidative Stress, Protein Multimerization.
Abstract
In eukaryotic cells, proteasomes exist primarily as 26S holoenzymes, the most efficient configuration for ubiquitinated protein degradation. Here, we show that acute oxidative stress caused by environmental insults or mitochondrial defects results in rapid disassembly of 26S proteasomes into intact 20S core and 19S regulatory particles. Consequently, polyubiquitinated substrates accumulate, mitochondrial networks fragment, and cellular reactive oxygen species (ROS) levels increase. Oxidation of cysteine residues is sufficient to induce proteasome disassembly, and spontaneous reassembly from existing components is observed both in vivo and in vitro upon reduction. Ubiquitin-dependent substrate turnover also resumes after treatment with antioxidants. Reversible attenuation of 26S proteasome activity induced by acute mitochondrial or oxidative stress may be a short-term response distinct from adaptation to long-term ROS exposure or changes during aging.
DOI: 10.1016/j.celrep.2014.04.030
PubMed: 24857655
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pubmed:24857655Le document en format XML
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Department of Biochemistry and Molecular Biology, Faculty of Health Sciences, Monash University, Melbourne, VIC 3800, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Department of Biology, Technion-Israel Institute of Technology, Haifa 32000, Israel; Department of Biochemistry and Molecular Biology, Faculty of Health Sciences, Monash University, Melbourne, VIC 3800</wicri:regionArea><wicri:noRegion>VIC 3800</wicri:noRegion></affiliation></author><author><name sortKey="Krutauz, Daria" sort="Krutauz, Daria" uniqKey="Krutauz D" first="Daria" last="Krutauz">Daria Krutauz</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biology, Technion-Israel Institute of Technology, Haifa 32000, Israel.</nlm:affiliation><country xml:lang="fr">Israël</country><wicri:regionArea>Department of Biology, Technion-Israel Institute of Technology, Haifa 32000</wicri:regionArea><wicri:noRegion>Haifa 32000</wicri:noRegion></affiliation></author><author><name sortKey="Segref, Alexandra" sort="Segref, Alexandra" uniqKey="Segref A" first="Alexandra" last="Segref">Alexandra Segref</name><affiliation wicri:level="3"><nlm:affiliation>Institute for Genetics, University of Cologne, Cologne 50674, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute for Genetics, University of Cologne, Cologne 50674</wicri:regionArea><placeName><region type="land" nuts="1">Rhénanie-du-Nord-Westphalie</region><region type="district" nuts="2">District de Cologne</region><settlement type="city">Cologne</settlement></placeName></affiliation></author><author><name sortKey="Rinaldi, Teresa" sort="Rinaldi, Teresa" uniqKey="Rinaldi T" first="Teresa" last="Rinaldi">Teresa Rinaldi</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biology and Biotechnology, University of Rome "La Sapienza," Rome 00185, Italy.</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Biology and Biotechnology, University of Rome "La Sapienza," Rome 00185</wicri:regionArea><wicri:noRegion>" Rome 00185</wicri:noRegion></affiliation></author><author><name sortKey="Erpapazoglou, Zoi" sort="Erpapazoglou, Zoi" uniqKey="Erpapazoglou Z" first="Zoi" last="Erpapazoglou">Zoi Erpapazoglou</name><affiliation wicri:level="1"><nlm:affiliation>Centre National de la Recherche Scientifique, UMR8226, IBPC, and Sorbonne Universités, UPMC, UMR8226, LBMCE, 75005 Paris, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Centre National de la Recherche Scientifique, UMR8226, IBPC, and Sorbonne Universités, UPMC, UMR8226, LBMCE, 75005 Paris</wicri:regionArea><wicri:noRegion>75005 Paris</wicri:noRegion><placeName><settlement type="city">Paris</settlement><region type="région" nuts="2">Île-de-France</region></placeName></affiliation></author><author><name sortKey="Cohen, Mickael" sort="Cohen, Mickael" uniqKey="Cohen M" first="Mickael" last="Cohen">Mickael Cohen</name><affiliation wicri:level="1"><nlm:affiliation>Centre National de la Recherche Scientifique, UMR8226, IBPC, and Sorbonne Universités, UPMC, UMR8226, LBMCE, 75005 Paris, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Centre National de la Recherche Scientifique, UMR8226, IBPC, and Sorbonne Universités, UPMC, UMR8226, LBMCE, 75005 Paris</wicri:regionArea><wicri:noRegion>75005 Paris</wicri:noRegion><placeName><settlement type="city">Paris</settlement><region type="région" nuts="2">Île-de-France</region></placeName></affiliation></author><author><name sortKey="Reis, Noa" sort="Reis, Noa" uniqKey="Reis N" first="Noa" last="Reis">Noa Reis</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biology, Technion-Israel Institute of Technology, Haifa 32000, Israel.</nlm:affiliation><country xml:lang="fr">Israël</country><wicri:regionArea>Department of Biology, Technion-Israel Institute of Technology, Haifa 32000</wicri:regionArea><wicri:noRegion>Haifa 32000</wicri:noRegion></affiliation></author><author><name sortKey="Hoppe, Thorsten" sort="Hoppe, Thorsten" uniqKey="Hoppe T" first="Thorsten" last="Hoppe">Thorsten Hoppe</name><affiliation wicri:level="3"><nlm:affiliation>Institute for Genetics, University of Cologne, Cologne 50674, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute for Genetics, University of Cologne, Cologne 50674</wicri:regionArea><placeName><region type="land" nuts="1">Rhénanie-du-Nord-Westphalie</region><region type="district" nuts="2">District de Cologne</region><settlement type="city">Cologne</settlement></placeName></affiliation></author><author><name sortKey="Glickman, Michael H" sort="Glickman, Michael H" uniqKey="Glickman M" first="Michael H" last="Glickman">Michael H. Glickman</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biology, Technion-Israel Institute of Technology, Haifa 32000, Israel. Electronic address: glickman@tx.technion.ac.il.</nlm:affiliation><country xml:lang="fr">Israël</country><wicri:regionArea>Department of Biology, Technion-Israel Institute of Technology, Haifa 32000</wicri:regionArea><wicri:noRegion>Haifa 32000</wicri:noRegion></affiliation></author></analytic><series><title level="j">Cell reports</title><idno type="eISSN">2211-1247</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Antioxidants (pharmacology)</term><term>Caenorhabditis elegans (metabolism)</term><term>Cell Line</term><term>Cricetinae</term><term>Cysteine (metabolism)</term><term>Mitochondria (drug effects)</term><term>Mitochondria (metabolism)</term><term>Oxidative Stress</term><term>Proteasome Endopeptidase Complex (metabolism)</term><term>Protein Multimerization</term><term>Reactive Oxygen Species (metabolism)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Ubiquitin (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Antioxydants (pharmacologie)</term><term>Caenorhabditis elegans (métabolisme)</term><term>Cricetinae</term><term>Cystéine (métabolisme)</term><term>Espèces réactives de l'oxygène (métabolisme)</term><term>Lignée cellulaire</term><term>Mitochondries ()</term><term>Mitochondries (métabolisme)</term><term>Multimérisation de protéines</term><term>Proteasome endopeptidase complex (métabolisme)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Stress oxydatif</term><term>Ubiquitine (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cysteine</term><term>Proteasome Endopeptidase Complex</term><term>Reactive Oxygen Species</term><term>Ubiquitin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antioxidants</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Mitochondria</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Caenorhabditis elegans</term><term>Mitochondria</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Caenorhabditis elegans</term><term>Cystéine</term><term>Espèces réactives de l'oxygène</term><term>Mitochondries</term><term>Proteasome endopeptidase complex</term><term>Saccharomyces cerevisiae</term><term>Ubiquitine</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antioxydants</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Cricetinae</term><term>Oxidative Stress</term><term>Protein Multimerization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cricetinae</term><term>Lignée cellulaire</term><term>Mitochondries</term><term>Multimérisation de protéines</term><term>Stress oxydatif</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In eukaryotic cells, proteasomes exist primarily as 26S holoenzymes, the most efficient configuration for ubiquitinated protein degradation. Here, we show that acute oxidative stress caused by environmental insults or mitochondrial defects results in rapid disassembly of 26S proteasomes into intact 20S core and 19S regulatory particles. Consequently, polyubiquitinated substrates accumulate, mitochondrial networks fragment, and cellular reactive oxygen species (ROS) levels increase. Oxidation of cysteine residues is sufficient to induce proteasome disassembly, and spontaneous reassembly from existing components is observed both in vivo and in vitro upon reduction. Ubiquitin-dependent substrate turnover also resumes after treatment with antioxidants. Reversible attenuation of 26S proteasome activity induced by acute mitochondrial or oxidative stress may be a short-term response distinct from adaptation to long-term ROS exposure or changes during aging.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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