PGC-1α buffers ROS-mediated removal of mitochondria during myogenesis
Identifieur interne : 000A82 ( Ncbi/Merge ); précédent : 000A81; suivant : 000A83PGC-1α buffers ROS-mediated removal of mitochondria during myogenesis
Auteurs : S. Baldelli [Italie] ; K. Aquilano [Italie] ; M R Ciriolo [Italie]Source :
- Cell Death & Disease [ 2041-4889 ] ; 2014.
Descripteurs français
- KwdFr :
- Animaux, Antioxydants (pharmacologie), Cellules musculaires (), Cellules musculaires (cytologie), Cellules musculaires (métabolisme), Chromanes (pharmacologie), Différenciation cellulaire, Dégradation des mitochondries, Développement musculaire (génétique), Espèces réactives de l'oxygène (antagonistes et inhibiteurs), Espèces réactives de l'oxygène (métabolisme), Facteurs de transcription (génétique), Facteurs de transcription (métabolisme), Facteurs de transcription Forkhead (génétique), Facteurs de transcription Forkhead (métabolisme), Lignée cellulaire, Mitochondries (), Mitochondries (métabolisme), Myogénine (génétique), Myogénine (métabolisme), Protein kinases (génétique), Protein kinases (métabolisme), Protéines associées aux microtubules (génétique), Protéines associées aux microtubules (métabolisme), Protéines du muscle (génétique), Protéines du muscle (métabolisme), Renouvellement des mitochondries (génétique), Régulation de l'expression des gènes au cours du développement, SKP cullin F-box protein ligases (génétique), SKP cullin F-box protein ligases (métabolisme), Souris, Stress oxydatif, Transduction du signal.
- MESH :
- antagonistes et inhibiteurs : Espèces réactives de l'oxygène.
- cytologie : Cellules musculaires.
- génétique : Développement musculaire, Facteurs de transcription, Facteurs de transcription Forkhead, Myogénine, Protein kinases, Protéines associées aux microtubules, Protéines du muscle, Renouvellement des mitochondries, SKP cullin F-box protein ligases.
- métabolisme : Cellules musculaires, Espèces réactives de l'oxygène, Facteurs de transcription, Facteurs de transcription Forkhead, Mitochondries, Myogénine, Protein kinases, Protéines associées aux microtubules, Protéines du muscle, SKP cullin F-box protein ligases.
- pharmacologie : Antioxydants, Chromanes.
- Animaux, Cellules musculaires, Différenciation cellulaire, Dégradation des mitochondries, Lignée cellulaire, Mitochondries, Régulation de l'expression des gènes au cours du développement, Souris, Stress oxydatif, Transduction du signal.
English descriptors
- KwdEn :
- Animals, Antioxidants (pharmacology), Cell Differentiation, Cell Line, Chromans (pharmacology), Forkhead Transcription Factors (genetics), Forkhead Transcription Factors (metabolism), Gene Expression Regulation, Developmental, Mice, Microtubule-Associated Proteins (genetics), Microtubule-Associated Proteins (metabolism), Mitochondria (drug effects), Mitochondria (metabolism), Mitochondrial Degradation, Mitochondrial Turnover (genetics), Muscle Cells (cytology), Muscle Cells (drug effects), Muscle Cells (metabolism), Muscle Development (genetics), Muscle Proteins (genetics), Muscle Proteins (metabolism), Myogenin (genetics), Myogenin (metabolism), Oxidative Stress, Protein Kinases (genetics), Protein Kinases (metabolism), Reactive Oxygen Species (antagonists & inhibitors), Reactive Oxygen Species (metabolism), SKP Cullin F-Box Protein Ligases (genetics), SKP Cullin F-Box Protein Ligases (metabolism), Signal Transduction, Transcription Factors (genetics), Transcription Factors (metabolism).
- MESH :
- chemical , antagonists & inhibitors : Reactive Oxygen Species.
- chemical , genetics : Forkhead Transcription Factors, Microtubule-Associated Proteins, Muscle Proteins, Myogenin, Protein Kinases, SKP Cullin F-Box Protein Ligases, Transcription Factors.
- chemical , metabolism : Forkhead Transcription Factors, Microtubule-Associated Proteins, Muscle Proteins, Myogenin, Protein Kinases, Reactive Oxygen Species, SKP Cullin F-Box Protein Ligases, Transcription Factors.
- chemical , pharmacology : Antioxidants, Chromans.
- cytology : Muscle Cells.
- drug effects : Mitochondria, Muscle Cells.
- genetics : Mitochondrial Turnover, Muscle Development.
- metabolism : Mitochondria, Muscle Cells.
- Animals, Cell Differentiation, Cell Line, Gene Expression Regulation, Developmental, Mice, Mitochondrial Degradation, Oxidative Stress, Signal Transduction.
Abstract
Mitochondrial biogenesis and mitophagy are recognized as critical processes underlying mitochondrial homeostasis. However, the molecular pathway(s) coordinating the balance between these cellular programs is still poorly investigated. Here, we show an induction of the nuclear and mitochondrial peroxisome proliferator-activated receptor gamma, coactivator 1 alpha (PGC-1
Url:
DOI: 10.1038/cddis.2014.458
PubMed: 25375380
PubMed Central: 4260723
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Links to Exploration step
PMC:4260723Le document en format XML
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<term>Chromans (pharmacology)</term>
<term>Forkhead Transcription Factors (genetics)</term>
<term>Forkhead Transcription Factors (metabolism)</term>
<term>Gene Expression Regulation, Developmental</term>
<term>Mice</term>
<term>Microtubule-Associated Proteins (genetics)</term>
<term>Microtubule-Associated Proteins (metabolism)</term>
<term>Mitochondria (drug effects)</term>
<term>Mitochondria (metabolism)</term>
<term>Mitochondrial Degradation</term>
<term>Mitochondrial Turnover (genetics)</term>
<term>Muscle Cells (cytology)</term>
<term>Muscle Cells (drug effects)</term>
<term>Muscle Cells (metabolism)</term>
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<term>Muscle Proteins (genetics)</term>
<term>Muscle Proteins (metabolism)</term>
<term>Myogenin (genetics)</term>
<term>Myogenin (metabolism)</term>
<term>Oxidative Stress</term>
<term>Protein Kinases (genetics)</term>
<term>Protein Kinases (metabolism)</term>
<term>Reactive Oxygen Species (antagonists & inhibitors)</term>
<term>Reactive Oxygen Species (metabolism)</term>
<term>SKP Cullin F-Box Protein Ligases (genetics)</term>
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<term>Signal Transduction</term>
<term>Transcription Factors (genetics)</term>
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<term>Antioxydants (pharmacologie)</term>
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<term>Cellules musculaires (cytologie)</term>
<term>Cellules musculaires (métabolisme)</term>
<term>Chromanes (pharmacologie)</term>
<term>Différenciation cellulaire</term>
<term>Dégradation des mitochondries</term>
<term>Développement musculaire (génétique)</term>
<term>Espèces réactives de l'oxygène (antagonistes et inhibiteurs)</term>
<term>Espèces réactives de l'oxygène (métabolisme)</term>
<term>Facteurs de transcription (génétique)</term>
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<term>Protéines du muscle (métabolisme)</term>
<term>Renouvellement des mitochondries (génétique)</term>
<term>Régulation de l'expression des gènes au cours du développement</term>
<term>SKP cullin F-box protein ligases (génétique)</term>
<term>SKP cullin F-box protein ligases (métabolisme)</term>
<term>Souris</term>
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<term>Muscle Proteins</term>
<term>Myogenin</term>
<term>Protein Kinases</term>
<term>SKP Cullin F-Box Protein Ligases</term>
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<term>Cell Differentiation</term>
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<term>Lignée cellulaire</term>
<term>Mitochondries</term>
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<front><div type="abstract" xml:lang="en"><p>Mitochondrial biogenesis and mitophagy are recognized as critical processes underlying mitochondrial homeostasis. However, the molecular pathway(s) coordinating the balance between these cellular programs is still poorly investigated. Here, we show an induction of the nuclear and mitochondrial peroxisome proliferator-activated receptor gamma, coactivator 1 alpha (PGC-1<italic>α</italic>
) during myogenesis, which in turn co-activates the transcription of nuclear and mtDNA-encoded mitochondrial genes. We demonstrate that PGC-1<italic>α</italic>
also buffers oxidative stress occurring during differentiation by promoting the expression of antioxidant enzymes. Indeed, by downregulating PGC-1<italic>α,</italic>
we observed an impairment of antioxidants expression, which was accompanied by a significant reactive oxygen species (ROS) burst and increase of oxidative damage to proteins. In parallel, we detected a decrease of mitochondrial mass and function as well as increased mitophagy through the ROS/FOXO1 pathway. Upon PGC-1<italic>α</italic>
downregulation, we found ROS-dependent nuclear translocation of FOXO1 and transcription of its downstream targets including mitophagic genes such as LC3 and PINK1. Such events were significantly reverted after treatment with the antioxidant Trolox, suggesting that PGC-1<italic>α</italic>
assures mitochondrial integrity by indirectly buffering ROS. Finally, the lack of PGC-1<italic>α</italic>
gave rise to a decrease in MYOG and a strong induction of atrophy-related ubiquitin ligases FBXO32 (FBXO32), indicative of a degenerative process. Overall, our results reveal that in myotubes, PGC-1<italic>α</italic>
takes center place in mitochondrial homeostasis during differentiation because of its ability to avoid ROS-mediated removal of mitochondria.</p>
</div>
</front>
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<author><name sortKey="Pagliei, B" uniqKey="Pagliei B">B Pagliei</name>
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<author><name sortKey="Uldry, M" uniqKey="Uldry M">M Uldry</name>
</author>
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<double pmid="25375380"><pmc><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">PGC-1<italic>α</italic>
buffers ROS-mediated removal of mitochondria during myogenesis</title>
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<country xml:lang="fr">Italie</country>
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<author><name sortKey="Ciriolo, M R" sort="Ciriolo, M R" uniqKey="Ciriolo M" first="M R" last="Ciriolo">M R Ciriolo</name>
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<country xml:lang="fr">Italie</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
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<country xml:lang="fr">Italie</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
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</titleStmt>
<publicationStmt><idno type="wicri:source">PMC</idno>
<idno type="pmid">25375380</idno>
<idno type="pmc">4260723</idno>
<idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4260723</idno>
<idno type="RBID">PMC:4260723</idno>
<idno type="doi">10.1038/cddis.2014.458</idno>
<date when="2014">2014</date>
<idno type="wicri:Area/Pmc/Corpus">000005</idno>
<idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000005</idno>
<idno type="wicri:Area/Pmc/Curation">000005</idno>
<idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000005</idno>
<idno type="wicri:Area/Pmc/Checkpoint">000141</idno>
<idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000141</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">PGC-1<italic>α</italic>
buffers ROS-mediated removal of mitochondria during myogenesis</title>
<author><name sortKey="Baldelli, S" sort="Baldelli, S" uniqKey="Baldelli S" first="S" last="Baldelli">S. Baldelli</name>
<affiliation wicri:level="1"><nlm:aff id="aff1"><institution>Scientific Institute for Research, Hospitalization and Health Care, Università Telematica San Raffaele Roma</institution>
, Via di Val Cannuta 247, Rome,<country>Italy</country>
</nlm:aff>
<country xml:lang="fr">Italie</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Aquilano, K" sort="Aquilano, K" uniqKey="Aquilano K" first="K" last="Aquilano">K. Aquilano</name>
<affiliation wicri:level="1"><nlm:aff id="aff2"><institution>Department of Biology, University of Rome “Tor Vergata”</institution>
, Via della Ricerca Scientifica 1, Rome,<country>Italy</country>
</nlm:aff>
<country xml:lang="fr">Italie</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
</affiliation>
</author>
<author><name sortKey="Ciriolo, M R" sort="Ciriolo, M R" uniqKey="Ciriolo M" first="M R" last="Ciriolo">M R Ciriolo</name>
<affiliation wicri:level="1"><nlm:aff id="aff2"><institution>Department of Biology, University of Rome “Tor Vergata”</institution>
, Via della Ricerca Scientifica 1, Rome,<country>Italy</country>
</nlm:aff>
<country xml:lang="fr">Italie</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
</affiliation>
<affiliation wicri:level="1"><nlm:aff id="aff3"><institution>IRCCS San Raffaele</institution>
, Via di Val Cannuta 247, Rome,<country>Italy</country>
</nlm:aff>
<country xml:lang="fr">Italie</country>
<wicri:regionArea># see nlm:aff country strict</wicri:regionArea>
</affiliation>
</author>
</analytic>
<series><title level="j">Cell Death & Disease</title>
<idno type="eISSN">2041-4889</idno>
<imprint><date when="2014">2014</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass></textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en"><p>Mitochondrial biogenesis and mitophagy are recognized as critical processes underlying mitochondrial homeostasis. However, the molecular pathway(s) coordinating the balance between these cellular programs is still poorly investigated. Here, we show an induction of the nuclear and mitochondrial peroxisome proliferator-activated receptor gamma, coactivator 1 alpha (PGC-1<italic>α</italic>
) during myogenesis, which in turn co-activates the transcription of nuclear and mtDNA-encoded mitochondrial genes. We demonstrate that PGC-1<italic>α</italic>
also buffers oxidative stress occurring during differentiation by promoting the expression of antioxidant enzymes. Indeed, by downregulating PGC-1<italic>α,</italic>
we observed an impairment of antioxidants expression, which was accompanied by a significant reactive oxygen species (ROS) burst and increase of oxidative damage to proteins. In parallel, we detected a decrease of mitochondrial mass and function as well as increased mitophagy through the ROS/FOXO1 pathway. Upon PGC-1<italic>α</italic>
downregulation, we found ROS-dependent nuclear translocation of FOXO1 and transcription of its downstream targets including mitophagic genes such as LC3 and PINK1. Such events were significantly reverted after treatment with the antioxidant Trolox, suggesting that PGC-1<italic>α</italic>
assures mitochondrial integrity by indirectly buffering ROS. Finally, the lack of PGC-1<italic>α</italic>
gave rise to a decrease in MYOG and a strong induction of atrophy-related ubiquitin ligases FBXO32 (FBXO32), indicative of a degenerative process. Overall, our results reveal that in myotubes, PGC-1<italic>α</italic>
takes center place in mitochondrial homeostasis during differentiation because of its ability to avoid ROS-mediated removal of mitochondria.</p>
</div>
</front>
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<pubmed><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">PGC-1α buffers ROS-mediated removal of mitochondria during myogenesis.</title>
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<affiliation wicri:level="3"><nlm:affiliation>Scientific Institute for Research, Hospitalization and Health Care, Università Telematica San Raffaele Roma, Via di Val Cannuta 247, Rome, Italy.</nlm:affiliation>
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<wicri:regionArea>Scientific Institute for Research, Hospitalization and Health Care, Università Telematica San Raffaele Roma, Via di Val Cannuta 247, Rome</wicri:regionArea>
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</placeName>
</affiliation>
</author>
<author><name sortKey="Aquilano, K" sort="Aquilano, K" uniqKey="Aquilano K" first="K" last="Aquilano">K. Aquilano</name>
<affiliation wicri:level="3"><nlm:affiliation>Department of Biology, University of Rome "Tor Vergata", Via della Ricerca Scientifica 1, Rome, Italy.</nlm:affiliation>
<country xml:lang="fr">Italie</country>
<wicri:regionArea>Department of Biology, University of Rome "Tor Vergata", Via della Ricerca Scientifica 1, Rome</wicri:regionArea>
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</placeName>
</affiliation>
</author>
<author><name sortKey="Ciriolo, M R" sort="Ciriolo, M R" uniqKey="Ciriolo M" first="M R" last="Ciriolo">M R Ciriolo</name>
<affiliation wicri:level="3"><nlm:affiliation>1] Department of Biology, University of Rome "Tor Vergata", Via della Ricerca Scientifica 1, Rome, Italy [2] IRCCS San Raffaele, Via di Val Cannuta 247, Rome, Italy.</nlm:affiliation>
<country xml:lang="fr">Italie</country>
<wicri:regionArea>1] Department of Biology, University of Rome "Tor Vergata", Via della Ricerca Scientifica 1, Rome, Italy [2] IRCCS San Raffaele, Via di Val Cannuta 247, Rome</wicri:regionArea>
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<author><name sortKey="Baldelli, S" sort="Baldelli, S" uniqKey="Baldelli S" first="S" last="Baldelli">S. Baldelli</name>
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</author>
<author><name sortKey="Aquilano, K" sort="Aquilano, K" uniqKey="Aquilano K" first="K" last="Aquilano">K. Aquilano</name>
<affiliation wicri:level="3"><nlm:affiliation>Department of Biology, University of Rome "Tor Vergata", Via della Ricerca Scientifica 1, Rome, Italy.</nlm:affiliation>
<country xml:lang="fr">Italie</country>
<wicri:regionArea>Department of Biology, University of Rome "Tor Vergata", Via della Ricerca Scientifica 1, Rome</wicri:regionArea>
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</affiliation>
</author>
<author><name sortKey="Ciriolo, M R" sort="Ciriolo, M R" uniqKey="Ciriolo M" first="M R" last="Ciriolo">M R Ciriolo</name>
<affiliation wicri:level="3"><nlm:affiliation>1] Department of Biology, University of Rome "Tor Vergata", Via della Ricerca Scientifica 1, Rome, Italy [2] IRCCS San Raffaele, Via di Val Cannuta 247, Rome, Italy.</nlm:affiliation>
<country xml:lang="fr">Italie</country>
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<series><title level="j">Cell death & disease</title>
<idno type="eISSN">2041-4889</idno>
<imprint><date when="2014" type="published">2014</date>
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<term>Antioxidants (pharmacology)</term>
<term>Cell Differentiation</term>
<term>Cell Line</term>
<term>Chromans (pharmacology)</term>
<term>Forkhead Transcription Factors (genetics)</term>
<term>Forkhead Transcription Factors (metabolism)</term>
<term>Gene Expression Regulation, Developmental</term>
<term>Mice</term>
<term>Microtubule-Associated Proteins (genetics)</term>
<term>Microtubule-Associated Proteins (metabolism)</term>
<term>Mitochondria (drug effects)</term>
<term>Mitochondria (metabolism)</term>
<term>Mitochondrial Degradation</term>
<term>Mitochondrial Turnover (genetics)</term>
<term>Muscle Cells (cytology)</term>
<term>Muscle Cells (drug effects)</term>
<term>Muscle Cells (metabolism)</term>
<term>Muscle Development (genetics)</term>
<term>Muscle Proteins (genetics)</term>
<term>Muscle Proteins (metabolism)</term>
<term>Myogenin (genetics)</term>
<term>Myogenin (metabolism)</term>
<term>Oxidative Stress</term>
<term>Protein Kinases (genetics)</term>
<term>Protein Kinases (metabolism)</term>
<term>Reactive Oxygen Species (antagonists & inhibitors)</term>
<term>Reactive Oxygen Species (metabolism)</term>
<term>SKP Cullin F-Box Protein Ligases (genetics)</term>
<term>SKP Cullin F-Box Protein Ligases (metabolism)</term>
<term>Signal Transduction</term>
<term>Transcription Factors (genetics)</term>
<term>Transcription Factors (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term>
<term>Antioxydants (pharmacologie)</term>
<term>Cellules musculaires ()</term>
<term>Cellules musculaires (cytologie)</term>
<term>Cellules musculaires (métabolisme)</term>
<term>Chromanes (pharmacologie)</term>
<term>Différenciation cellulaire</term>
<term>Dégradation des mitochondries</term>
<term>Développement musculaire (génétique)</term>
<term>Espèces réactives de l'oxygène (antagonistes et inhibiteurs)</term>
<term>Espèces réactives de l'oxygène (métabolisme)</term>
<term>Facteurs de transcription (génétique)</term>
<term>Facteurs de transcription (métabolisme)</term>
<term>Facteurs de transcription Forkhead (génétique)</term>
<term>Facteurs de transcription Forkhead (métabolisme)</term>
<term>Lignée cellulaire</term>
<term>Mitochondries ()</term>
<term>Mitochondries (métabolisme)</term>
<term>Myogénine (génétique)</term>
<term>Myogénine (métabolisme)</term>
<term>Protein kinases (génétique)</term>
<term>Protein kinases (métabolisme)</term>
<term>Protéines associées aux microtubules (génétique)</term>
<term>Protéines associées aux microtubules (métabolisme)</term>
<term>Protéines du muscle (génétique)</term>
<term>Protéines du muscle (métabolisme)</term>
<term>Renouvellement des mitochondries (génétique)</term>
<term>Régulation de l'expression des gènes au cours du développement</term>
<term>SKP cullin F-box protein ligases (génétique)</term>
<term>SKP cullin F-box protein ligases (métabolisme)</term>
<term>Souris</term>
<term>Stress oxydatif</term>
<term>Transduction du signal</term>
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</keywords>
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<term>Microtubule-Associated Proteins</term>
<term>Muscle Proteins</term>
<term>Myogenin</term>
<term>Protein Kinases</term>
<term>SKP Cullin F-Box Protein Ligases</term>
<term>Transcription Factors</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Forkhead Transcription Factors</term>
<term>Microtubule-Associated Proteins</term>
<term>Muscle Proteins</term>
<term>Myogenin</term>
<term>Protein Kinases</term>
<term>Reactive Oxygen Species</term>
<term>SKP Cullin F-Box Protein Ligases</term>
<term>Transcription Factors</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antioxidants</term>
<term>Chromans</term>
</keywords>
<keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Espèces réactives de l'oxygène</term>
</keywords>
<keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Cellules musculaires</term>
</keywords>
<keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Muscle Cells</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Mitochondria</term>
<term>Muscle Cells</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Mitochondrial Turnover</term>
<term>Muscle Development</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Développement musculaire</term>
<term>Facteurs de transcription</term>
<term>Facteurs de transcription Forkhead</term>
<term>Myogénine</term>
<term>Protein kinases</term>
<term>Protéines associées aux microtubules</term>
<term>Protéines du muscle</term>
<term>Renouvellement des mitochondries</term>
<term>SKP cullin F-box protein ligases</term>
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<term>Muscle Cells</term>
</keywords>
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<term>Espèces réactives de l'oxygène</term>
<term>Facteurs de transcription</term>
<term>Facteurs de transcription Forkhead</term>
<term>Mitochondries</term>
<term>Myogénine</term>
<term>Protein kinases</term>
<term>Protéines associées aux microtubules</term>
<term>Protéines du muscle</term>
<term>SKP cullin F-box protein ligases</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antioxydants</term>
<term>Chromanes</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Cell Differentiation</term>
<term>Cell Line</term>
<term>Gene Expression Regulation, Developmental</term>
<term>Mice</term>
<term>Mitochondrial Degradation</term>
<term>Oxidative Stress</term>
<term>Signal Transduction</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Cellules musculaires</term>
<term>Différenciation cellulaire</term>
<term>Dégradation des mitochondries</term>
<term>Lignée cellulaire</term>
<term>Mitochondries</term>
<term>Régulation de l'expression des gènes au cours du développement</term>
<term>Souris</term>
<term>Stress oxydatif</term>
<term>Transduction du signal</term>
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<front><div type="abstract" xml:lang="en">Mitochondrial biogenesis and mitophagy are recognized as critical processes underlying mitochondrial homeostasis. However, the molecular pathway(s) coordinating the balance between these cellular programs is still poorly investigated. Here, we show an induction of the nuclear and mitochondrial peroxisome proliferator-activated receptor gamma, coactivator 1 alpha (PGC-1α) during myogenesis, which in turn co-activates the transcription of nuclear and mtDNA-encoded mitochondrial genes. We demonstrate that PGC-1α also buffers oxidative stress occurring during differentiation by promoting the expression of antioxidant enzymes. Indeed, by downregulating PGC-1α, we observed an impairment of antioxidants expression, which was accompanied by a significant reactive oxygen species (ROS) burst and increase of oxidative damage to proteins. In parallel, we detected a decrease of mitochondrial mass and function as well as increased mitophagy through the ROS/FOXO1 pathway. Upon PGC-1α downregulation, we found ROS-dependent nuclear translocation of FOXO1 and transcription of its downstream targets including mitophagic genes such as LC3 and PINK1. Such events were significantly reverted after treatment with the antioxidant Trolox, suggesting that PGC-1α assures mitochondrial integrity by indirectly buffering ROS. Finally, the lack of PGC-1α gave rise to a decrease in MYOG and a strong induction of atrophy-related ubiquitin ligases FBXO32 (FBXO32), indicative of a degenerative process. Overall, our results reveal that in myotubes, PGC-1α takes center place in mitochondrial homeostasis during differentiation because of its ability to avoid ROS-mediated removal of mitochondria.</div>
</front>
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