Parkin maintains mitochondrial levels of the protective Parkinson's disease-related enzyme 17-β hydroxysteroid dehydrogenase type 10.
Identifieur interne : 000277 ( PubMed/Curation ); précédent : 000276; suivant : 000278Parkin maintains mitochondrial levels of the protective Parkinson's disease-related enzyme 17-β hydroxysteroid dehydrogenase type 10.
Auteurs : G. Bertolin [France] ; M. Jacoupy [France] ; S. Traver [France] ; R. Ferrando-Miguel [France] ; T. Saint Georges [France] ; K. Grenier [Canada] ; H. Ardila-Osorio [France] ; M-P Muriel [France] ; H. Takahashi [Japon] ; A J Lees [Royaume-Uni] ; C. Gautier [France] ; D. Guedin [France] ; F. Coge [France] ; E A Fon [Canada] ; A. Brice [France] ; O. Corti [France]Source :
- Cell death and differentiation [ 1476-5403 ] ; 2015.
English descriptors
- KwdEn :
- 3-Hydroxyacyl CoA Dehydrogenases (genetics), 3-Hydroxyacyl CoA Dehydrogenases (metabolism), Animals, Brain (metabolism), Brain (physiopathology), Gene Expression Regulation, Humans, Mice, Mitochondria (metabolism), Mitochondria (physiology), Mitochondrial Membrane Transport Proteins (metabolism), Mitochondrial Proteins (metabolism), Mitochondrial Turnover, Mutation, Parkinson Disease (metabolism), Parkinson Disease (physiopathology), Rats, Ubiquitin-Protein Ligases (genetics), Ubiquitin-Protein Ligases (metabolism), Ubiquitination.
- MESH :
- chemical , genetics : 3-Hydroxyacyl CoA Dehydrogenases, Ubiquitin-Protein Ligases.
- chemical , metabolism : 3-Hydroxyacyl CoA Dehydrogenases, Mitochondrial Membrane Transport Proteins, Mitochondrial Proteins, Ubiquitin-Protein Ligases.
- metabolism : Brain, Mitochondria, Parkinson Disease.
- physiology : Mitochondria.
- physiopathology : Brain, Parkinson Disease.
- Animals, Gene Expression Regulation, Humans, Mice, Mitochondrial Turnover, Mutation, Rats, Ubiquitination.
Abstract
Mutations of the PARK2 and PINK1 genes, encoding the cytosolic E3 ubiquitin-protein ligase Parkin and the mitochondrial serine/threonine kinase PINK1, respectively, cause autosomal recessive early-onset Parkinson's disease (PD). Parkin and PINK1 cooperate in a biochemical mitochondrial quality control pathway regulating mitochondrial morphology, dynamics and clearance. This study identifies the multifunctional PD-related mitochondrial matrix enzyme 17-β hydroxysteroid dehydrogenase type 10 (HSD17B10) as a new Parkin substrate. Parkin overproduction in cells increased mitochondrial HSD17B10 abundance by a mechanism involving ubiquitin chain extension, whereas PARK2 downregulation or deficiency caused mitochondrial HSD17B10 depletion in cells and mice. HSD17B10 levels were also found to be low in the brains of PD patients with PARK2 mutations. Confocal and Förster resonance energy transfer (FRET) microscopy revealed that HSD17B10 recruited Parkin to the translocase of the outer membrane (TOM), close to PINK1, both in functional mitochondria and after the collapse of mitochondrial membrane potential (ΔΨm). PD-causing PARK2 mutations impaired interaction with HSD17B10 and the HSD17B10-dependent mitochondrial translocation of Parkin. HSD17B10 overproduction promoted mitochondrial elongation and mitigated CCCP-induced mitochondrial degradation independently of enzymatic activity. These effects were abolished by overproduction of the fission-promiting dynamin-related protein 1 (Drp1). By contrast, siRNA-mediated HSD17B10 silencing enhanced mitochondrial fission and mitophagy. These findings suggest that the maintenance of appropriate mitochondrial HSD17B10 levels is one of the mechanisms by which Parkin preserves mitochondrial quality. The loss of this protective mechanism may contribute to mitochondrial dysfunction and neuronal degeneration in autosomal recessive PD.
DOI: 10.1038/cdd.2014.224
PubMed: 25591737
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Bertolin</name><affiliation wicri:level="1"><nlm:affiliation>Inserm, U1127, 75013 Paris, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Inserm, U1127, 75013 Paris</wicri:regionArea></affiliation></author><author><name sortKey="Jacoupy, M" sort="Jacoupy, M" uniqKey="Jacoupy M" first="M" last="Jacoupy">M. Jacoupy</name><affiliation wicri:level="1"><nlm:affiliation>Inserm, U1127, 75013 Paris, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Inserm, U1127, 75013 Paris</wicri:regionArea></affiliation></author><author><name sortKey="Traver, S" sort="Traver, S" uniqKey="Traver S" first="S" last="Traver">S. Traver</name><affiliation wicri:level="1"><nlm:affiliation>CHU Montpellier, Institute for Research in Biotherapy, Saint-Eloi Hospital, Montpellier, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>CHU Montpellier, Institute for Research in Biotherapy, Saint-Eloi Hospital, Montpellier</wicri:regionArea></affiliation></author><author><name sortKey="Ferrando Miguel, R" sort="Ferrando Miguel, R" uniqKey="Ferrando Miguel R" first="R" last="Ferrando-Miguel">R. Ferrando-Miguel</name><affiliation wicri:level="1"><nlm:affiliation>Inserm, U1127, 75013 Paris, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Inserm, U1127, 75013 Paris</wicri:regionArea></affiliation></author><author><name sortKey="Saint Georges, T" sort="Saint Georges, T" uniqKey="Saint Georges T" first="T" last="Saint Georges">T. Saint Georges</name><affiliation wicri:level="1"><nlm:affiliation>Inserm, U1127, 75013 Paris, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Inserm, U1127, 75013 Paris</wicri:regionArea></affiliation></author><author><name sortKey="Grenier, K" sort="Grenier, K" uniqKey="Grenier K" first="K" last="Grenier">K. Grenier</name><affiliation wicri:level="1"><nlm:affiliation>McGill Parkinson Program, Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>McGill Parkinson Program, Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec</wicri:regionArea></affiliation></author><author><name sortKey="Ardila Osorio, H" sort="Ardila Osorio, H" uniqKey="Ardila Osorio H" first="H" last="Ardila-Osorio">H. Ardila-Osorio</name><affiliation wicri:level="1"><nlm:affiliation>Inserm, U1127, 75013 Paris, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Inserm, U1127, 75013 Paris</wicri:regionArea></affiliation></author><author><name sortKey="Muriel, M P" sort="Muriel, M P" uniqKey="Muriel M" first="M-P" last="Muriel">M-P Muriel</name><affiliation wicri:level="1"><nlm:affiliation>Inserm, U1127, 75013 Paris, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Inserm, U1127, 75013 Paris</wicri:regionArea></affiliation></author><author><name sortKey="Takahashi, H" sort="Takahashi, H" uniqKey="Takahashi H" first="H" last="Takahashi">H. Takahashi</name><affiliation wicri:level="1"><nlm:affiliation>Department of Pathology, Brain Research Institute, University of Niigata, Niigata, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Pathology, Brain Research Institute, University of Niigata, Niigata</wicri:regionArea></affiliation></author><author><name sortKey="Lees, A J" sort="Lees, A J" uniqKey="Lees A" first="A J" last="Lees">A J Lees</name><affiliation wicri:level="1"><nlm:affiliation>Reta Lila Weston Institute for Neurological Studies, Institute of Neurology, University College London, London, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Reta Lila Weston Institute for Neurological Studies, Institute of Neurology, University College London, London</wicri:regionArea></affiliation></author><author><name sortKey="Gautier, C" sort="Gautier, C" uniqKey="Gautier C" first="C" last="Gautier">C. Gautier</name><affiliation wicri:level="1"><nlm:affiliation>Laboratoire Chémogénétique Servier-Diverchim, Institut du Cerveau et de la Moelle épinière, ICM, Paris, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire Chémogénétique Servier-Diverchim, Institut du Cerveau et de la Moelle épinière, ICM, Paris</wicri:regionArea></affiliation></author><author><name sortKey="Guedin, D" sort="Guedin, D" uniqKey="Guedin D" first="D" last="Guedin">D. Guedin</name><affiliation wicri:level="1"><nlm:affiliation>Laboratoire Chémogénétique Servier-Diverchim, Institut du Cerveau et de la Moelle épinière, ICM, Paris, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire Chémogénétique Servier-Diverchim, Institut du Cerveau et de la Moelle épinière, ICM, Paris</wicri:regionArea></affiliation></author><author><name sortKey="Coge, F" sort="Coge, F" uniqKey="Coge F" first="F" last="Coge">F. Coge</name><affiliation wicri:level="1"><nlm:affiliation>Laboratoire Chémogénétique Servier-Diverchim, Institut du Cerveau et de la Moelle épinière, ICM, Paris, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire Chémogénétique Servier-Diverchim, Institut du Cerveau et de la Moelle épinière, ICM, Paris</wicri:regionArea></affiliation></author><author><name sortKey="Fon, E A" sort="Fon, E A" uniqKey="Fon E" first="E A" last="Fon">E A Fon</name><affiliation wicri:level="1"><nlm:affiliation>McGill Parkinson Program, Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>McGill Parkinson Program, Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec</wicri:regionArea></affiliation></author><author><name sortKey="Brice, A" sort="Brice, A" uniqKey="Brice A" first="A" last="Brice">A. Brice</name><affiliation wicri:level="1"><nlm:affiliation>Inserm, U1127, 75013 Paris, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Inserm, U1127, 75013 Paris</wicri:regionArea></affiliation></author><author><name sortKey="Corti, O" sort="Corti, O" uniqKey="Corti O" first="O" last="Corti">O. Corti</name><affiliation wicri:level="1"><nlm:affiliation>Inserm, U1127, 75013 Paris, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Inserm, U1127, 75013 Paris</wicri:regionArea></affiliation></author></analytic><series><title level="j">Cell death and differentiation</title><idno type="eISSN">1476-5403</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>3-Hydroxyacyl CoA Dehydrogenases (genetics)</term><term>3-Hydroxyacyl CoA Dehydrogenases (metabolism)</term><term>Animals</term><term>Brain (metabolism)</term><term>Brain (physiopathology)</term><term>Gene Expression Regulation</term><term>Humans</term><term>Mice</term><term>Mitochondria (metabolism)</term><term>Mitochondria (physiology)</term><term>Mitochondrial Membrane Transport Proteins (metabolism)</term><term>Mitochondrial Proteins (metabolism)</term><term>Mitochondrial Turnover</term><term>Mutation</term><term>Parkinson Disease (metabolism)</term><term>Parkinson Disease (physiopathology)</term><term>Rats</term><term>Ubiquitin-Protein Ligases (genetics)</term><term>Ubiquitin-Protein Ligases (metabolism)</term><term>Ubiquitination</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>3-Hydroxyacyl CoA Dehydrogenases</term><term>Ubiquitin-Protein Ligases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>3-Hydroxyacyl CoA Dehydrogenases</term><term>Mitochondrial Membrane Transport Proteins</term><term>Mitochondrial Proteins</term><term>Ubiquitin-Protein Ligases</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Brain</term><term>Mitochondria</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Mitochondria</term></keywords><keywords scheme="MESH" qualifier="physiopathology" xml:lang="en"><term>Brain</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Gene Expression Regulation</term><term>Humans</term><term>Mice</term><term>Mitochondrial Turnover</term><term>Mutation</term><term>Rats</term><term>Ubiquitination</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Mutations of the PARK2 and PINK1 genes, encoding the cytosolic E3 ubiquitin-protein ligase Parkin and the mitochondrial serine/threonine kinase PINK1, respectively, cause autosomal recessive early-onset Parkinson's disease (PD). Parkin and PINK1 cooperate in a biochemical mitochondrial quality control pathway regulating mitochondrial morphology, dynamics and clearance. This study identifies the multifunctional PD-related mitochondrial matrix enzyme 17-β hydroxysteroid dehydrogenase type 10 (HSD17B10) as a new Parkin substrate. Parkin overproduction in cells increased mitochondrial HSD17B10 abundance by a mechanism involving ubiquitin chain extension, whereas PARK2 downregulation or deficiency caused mitochondrial HSD17B10 depletion in cells and mice. HSD17B10 levels were also found to be low in the brains of PD patients with PARK2 mutations. Confocal and Förster resonance energy transfer (FRET) microscopy revealed that HSD17B10 recruited Parkin to the translocase of the outer membrane (TOM), close to PINK1, both in functional mitochondria and after the collapse of mitochondrial membrane potential (ΔΨm). PD-causing PARK2 mutations impaired interaction with HSD17B10 and the HSD17B10-dependent mitochondrial translocation of Parkin. HSD17B10 overproduction promoted mitochondrial elongation and mitigated CCCP-induced mitochondrial degradation independently of enzymatic activity. These effects were abolished by overproduction of the fission-promiting dynamin-related protein 1 (Drp1). By contrast, siRNA-mediated HSD17B10 silencing enhanced mitochondrial fission and mitophagy. These findings suggest that the maintenance of appropriate mitochondrial HSD17B10 levels is one of the mechanisms by which Parkin preserves mitochondrial quality. The loss of this protective mechanism may contribute to mitochondrial dysfunction and neuronal degeneration in autosomal recessive PD.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25591737</PMID><DateCreated><Year>2015</Year><Month>09</Month><Day>08</Day></DateCreated><DateCompleted><Year>2016</Year><Month>06</Month><Day>14</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1476-5403</ISSN><JournalIssue CitedMedium="Internet"><Volume>22</Volume><Issue>10</Issue><PubDate><Year>2015</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Cell death and differentiation</Title><ISOAbbreviation>Cell Death Differ.</ISOAbbreviation></Journal><ArticleTitle>Parkin maintains mitochondrial levels of the protective Parkinson's disease-related enzyme 17-β hydroxysteroid dehydrogenase type 10.</ArticleTitle><Pagination><MedlinePgn>1563-76</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1038/cdd.2014.224</ELocationID><Abstract><AbstractText>Mutations of the PARK2 and PINK1 genes, encoding the cytosolic E3 ubiquitin-protein ligase Parkin and the mitochondrial serine/threonine kinase PINK1, respectively, cause autosomal recessive early-onset Parkinson's disease (PD). Parkin and PINK1 cooperate in a biochemical mitochondrial quality control pathway regulating mitochondrial morphology, dynamics and clearance. This study identifies the multifunctional PD-related mitochondrial matrix enzyme 17-β hydroxysteroid dehydrogenase type 10 (HSD17B10) as a new Parkin substrate. Parkin overproduction in cells increased mitochondrial HSD17B10 abundance by a mechanism involving ubiquitin chain extension, whereas PARK2 downregulation or deficiency caused mitochondrial HSD17B10 depletion in cells and mice. HSD17B10 levels were also found to be low in the brains of PD patients with PARK2 mutations. Confocal and Förster resonance energy transfer (FRET) microscopy revealed that HSD17B10 recruited Parkin to the translocase of the outer membrane (TOM), close to PINK1, both in functional mitochondria and after the collapse of mitochondrial membrane potential (ΔΨm). PD-causing PARK2 mutations impaired interaction with HSD17B10 and the HSD17B10-dependent mitochondrial translocation of Parkin. HSD17B10 overproduction promoted mitochondrial elongation and mitigated CCCP-induced mitochondrial degradation independently of enzymatic activity. These effects were abolished by overproduction of the fission-promiting dynamin-related protein 1 (Drp1). By contrast, siRNA-mediated HSD17B10 silencing enhanced mitochondrial fission and mitophagy. These findings suggest that the maintenance of appropriate mitochondrial HSD17B10 levels is one of the mechanisms by which Parkin preserves mitochondrial quality. The loss of this protective mechanism may contribute to mitochondrial dysfunction and neuronal degeneration in autosomal recessive PD.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bertolin</LastName><ForeName>G</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Inserm, U1127, 75013 Paris, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>CNRS, UMR 7225, 75013 Paris, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Sorbonne Universités, UPMC Univ Paris 06, UMR S 1127, 75013 Paris, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Institut du Cerveau et de la Moelle épinière, ICM, 75013 Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jacoupy</LastName><ForeName>M</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Inserm, U1127, 75013 Paris, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>CNRS, UMR 7225, 75013 Paris, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Sorbonne Universités, UPMC Univ Paris 06, UMR S 1127, 75013 Paris, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Institut du Cerveau et de la Moelle épinière, ICM, 75013 Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Traver</LastName><ForeName>S</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>CHU Montpellier, Institute for Research in Biotherapy, Saint-Eloi Hospital, Montpellier, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ferrando-Miguel</LastName><ForeName>R</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Inserm, U1127, 75013 Paris, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>CNRS, UMR 7225, 75013 Paris, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Sorbonne Universités, UPMC Univ Paris 06, UMR S 1127, 75013 Paris, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Institut du Cerveau et de la Moelle épinière, ICM, 75013 Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Saint Georges</LastName><ForeName>T</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Inserm, U1127, 75013 Paris, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>CNRS, UMR 7225, 75013 Paris, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Sorbonne Universités, UPMC Univ Paris 06, UMR S 1127, 75013 Paris, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Institut du Cerveau et de la Moelle épinière, ICM, 75013 Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Grenier</LastName><ForeName>K</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>McGill Parkinson Program, Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ardila-Osorio</LastName><ForeName>H</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Inserm, U1127, 75013 Paris, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>CNRS, UMR 7225, 75013 Paris, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Sorbonne Universités, UPMC Univ Paris 06, UMR S 1127, 75013 Paris, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Institut du Cerveau et de la Moelle épinière, ICM, 75013 Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Muriel</LastName><ForeName>M-P</ForeName><Initials>MP</Initials><AffiliationInfo><Affiliation>Inserm, U1127, 75013 Paris, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>CNRS, UMR 7225, 75013 Paris, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Sorbonne Universités, UPMC Univ Paris 06, UMR S 1127, 75013 Paris, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Institut du Cerveau et de la Moelle épinière, ICM, 75013 Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Takahashi</LastName><ForeName>H</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Department of Pathology, Brain Research Institute, University of Niigata, Niigata, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lees</LastName><ForeName>A J</ForeName><Initials>AJ</Initials><AffiliationInfo><Affiliation>Reta Lila Weston Institute for Neurological Studies, Institute of Neurology, University College London, London, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gautier</LastName><ForeName>C</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Laboratoire Chémogénétique Servier-Diverchim, Institut du Cerveau et de la Moelle épinière, ICM, Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Guedin</LastName><ForeName>D</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Laboratoire Chémogénétique Servier-Diverchim, Institut du Cerveau et de la Moelle épinière, ICM, Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Coge</LastName><ForeName>F</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Laboratoire Chémogénétique Servier-Diverchim, Institut du Cerveau et de la Moelle épinière, ICM, Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fon</LastName><ForeName>E A</ForeName><Initials>EA</Initials><AffiliationInfo><Affiliation>McGill Parkinson Program, Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Brice</LastName><ForeName>A</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Inserm, U1127, 75013 Paris, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>CNRS, UMR 7225, 75013 Paris, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Sorbonne Universités, UPMC Univ Paris 06, UMR S 1127, 75013 Paris, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Institut du Cerveau et de la Moelle épinière, ICM, 75013 Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Corti</LastName><ForeName>O</ForeName><Initials>O</Initials><AffiliationInfo><Affiliation>Inserm, U1127, 75013 Paris, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>CNRS, UMR 7225, 75013 Paris, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Sorbonne Universités, UPMC Univ Paris 06, UMR S 1127, 75013 Paris, France.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Institut du Cerveau et de la Moelle épinière, ICM, 75013 Paris, France.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>01</Month><Day>16</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Cell Death Differ</MedlineTA><NlmUniqueID>9437445</NlmUniqueID><ISSNLinking>1350-9047</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D033681">Mitochondrial Membrane Transport Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D024101">Mitochondrial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 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26;340(6131):471-5</RefSource><PMID Version="1">23620051</PMID></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D015094" MajorTopicYN="N">3-Hydroxyacyl CoA Dehydrogenases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001921" MajorTopicYN="N">Brain</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000503" MajorTopicYN="N">physiopathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005786" MajorTopicYN="N">Gene Expression Regulation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051379" 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