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
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: Pour aller vers cette notice dans l'étape Curation :000278
Links to Exploration step
pubmed:25591737Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Parkin maintains mitochondrial levels of the protective Parkinson's disease-related enzyme 17-β hydroxysteroid dehydrogenase type 10.</title>
<author><name sortKey="Bertolin, G" sort="Bertolin, G" uniqKey="Bertolin G" first="G" last="Bertolin">G. 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>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2015">2015</date>
<idno type="RBID">pubmed:25591737</idno>
<idno type="pmid">25591737</idno>
<idno type="doi">10.1038/cdd.2014.224</idno>
<idno type="wicri:Area/PubMed/Corpus">000278</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000278</idno>
<idno type="wicri:Area/PubMed/Curation">000277</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000277</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">Parkin maintains mitochondrial levels of the protective Parkinson's disease-related enzyme 17-β hydroxysteroid dehydrogenase type 10.</title>
<author><name sortKey="Bertolin, G" sort="Bertolin, G" uniqKey="Bertolin G" first="G" last="Bertolin">G. 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 1.1.1.-</RegistryNumber>
<NameOfSubstance UI="D015094">3-Hydroxyacyl CoA Dehydrogenases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 1.1.1.35</RegistryNumber>
<NameOfSubstance UI="C108634">HSD17B10 protein, human</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.3.2.27</RegistryNumber>
<NameOfSubstance UI="D044767">Ubiquitin-Protein Ligases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.3.2.27</RegistryNumber>
<NameOfSubstance UI="C111567">parkin protein</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>Nature. 2013 Apr 18;496(7445):372-6</RefSource>
<PMID Version="1">23503661</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Hum Mol Genet. 2003 Mar 1;12(5):517-26</RefSource>
<PMID Version="1">12588799</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Pediatr Res. 2000 Dec;48(6):852-5</RefSource>
<PMID Version="1">11102558</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Proc Natl Acad Sci U S A. 2008 Sep 23;105(38):14503-8</RefSource>
<PMID Version="1">18799731</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Proc Natl Acad Sci U S A. 2008 Oct 14;105(41):15803-8</RefSource>
<PMID Version="1">18838687</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Cell. 2008 Oct 31;135(3):462-74</RefSource>
<PMID Version="1">18984158</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Cell Biol. 2008 Dec 1;183(5):795-803</RefSource>
<PMID Version="1">19029340</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>EMBO J. 2009 Jun 3;28(11):1589-600</RefSource>
<PMID Version="1">19360003</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Cell. 2009 Aug 21;138(4):628-44</RefSource>
<PMID Version="1">19703392</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Proc Natl Acad Sci U S A. 2010 Jan 5;107(1):378-83</RefSource>
<PMID Version="1">19966284</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nat Cell Biol. 2010 Feb;12(2):119-31</RefSource>
<PMID Version="1">20098416</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>PLoS Biol. 2010 Jan;8(1):e1000298</RefSource>
<PMID Version="1">20126261</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>EMBO Mol Med. 2010 Feb;2(2):51-62</RefSource>
<PMID Version="1">20077426</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Cell Biol. 2010 Apr 19;189(2):211-21</RefSource>
<PMID Version="1">20404107</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Cell Biol. 2010 Dec 27;191(7):1367-80</RefSource>
<PMID Version="1">21173115</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Hum Mol Genet. 2011 May 1;20(9):1726-37</RefSource>
<PMID Version="1">21296869</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nat Cell Biol. 2011 May;13(5):589-98</RefSource>
<PMID Version="1">21478857</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 2011 Jun 3;286(22):19630-40</RefSource>
<PMID Version="1">21454557</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Proc Natl Acad Sci U S A. 2011 Jun 21;108(25):10190-5</RefSource>
<PMID Version="1">21646527</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Physiol Rev. 2011 Oct;91(4):1161-218</RefSource>
<PMID Version="1">22013209</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Inherit Metab Dis. 2012 Jan;35(1):81-9</RefSource>
<PMID Version="1">22127393</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Dev Cell. 2012 Feb 14;22(2):320-33</RefSource>
<PMID Version="1">22280891</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>EMBO Rep. 2012 Apr;13(4):378-85</RefSource>
<PMID Version="1">22354088</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Neurosci. 2007 Jul 18;27(29):7827-37</RefSource>
<PMID Version="1">17634376</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nat Rev Mol Cell Biol. 2007 Nov;8(11):870-9</RefSource>
<PMID Version="1">17928812</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>EMBO J. 2008 Jan 23;27(2):433-46</RefSource>
<PMID Version="1">18200046</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Curr Protoc Cell Biol. 2006 Oct;Chapter 17:Unit 17.9</RefSource>
<PMID Version="1">18228480</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Proc Natl Acad Sci U S A. 2008 Feb 5;105(5):1638-43</RefSource>
<PMID Version="1">18230723</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Mol Cell Biol. 2013 Jun;33(11):2136-48</RefSource>
<PMID Version="1">23508107</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>EMBO J. 2013 Jul 31;32(15):2087-9</RefSource>
<PMID Version="1">23852447</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Autophagy. 2013 Nov 1;9(11):1801-17</RefSource>
<PMID Version="1">24149440</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Autophagy. 2013 Nov 1;9(11):1750-7</RefSource>
<PMID Version="1">24149988</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Hum Mol Genet. 2014 Jan 1;23(1):145-56</RefSource>
<PMID Version="1">23962723</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>PLoS One. 2014;9(6):e99898</RefSource>
<PMID Version="1">24959870</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Biochim Biophys Acta. 2014 Sep;1843(9):2012-26</RefSource>
<PMID Version="1">24878071</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Steroid Biochem Mol Biol. 2014 Sep;143:460-72</RefSource>
<PMID Version="1">25007702</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nat Biotechnol. 2012 Nov;30(11):1143-8</RefSource>
<PMID Version="1">23086203</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Cell Sci. 2002 Apr 15;115(Pt 8):1663-74</RefSource>
<PMID Version="1">11950885</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Proc Natl Acad Sci U S A. 2008 May 13;105(19):7070-5</RefSource>
<PMID Version="1">18443288</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Hum Mol Genet. 2003 Sep 15;12(18):2277-91</RefSource>
<PMID Version="1">12915482</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 2003 Oct 31;278(44):43628-35</RefSource>
<PMID Version="1">12930822</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Science. 2004 Apr 16;304(5669):448-52</RefSource>
<PMID Version="1">15087549</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 2004 Apr 30;279(18):18614-22</RefSource>
<PMID Version="1">14985362</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Ann Neurol. 2004 Jul;56(1):51-60</RefSource>
<PMID Version="1">15236401</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Proc Natl Acad Sci U S A. 2004 Jul 20;101(29):10744-9</RefSource>
<PMID Version="1">15249681</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nature. 1997 Oct 16;389(6652):689-95</RefSource>
<PMID Version="1">9338779</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Proc Natl Acad Sci U S A. 2005 Feb 8;102(6):2174-9</RefSource>
<PMID Version="1">15684050</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Am J Physiol Cell Physiol. 2005 Oct;289(4):C881-90</RefSource>
<PMID Version="1">15901599</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Neurochem. 2005 Dec;95(5):1259-76</RefSource>
<PMID Version="1">16150055</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Hum Mol Genet. 2006 Jul 1;15(13):2059-75</RefSource>
<PMID Version="1">16714300</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nature. 2006 Jun 29;441(7097):1157-61</RefSource>
<PMID Version="1">16672980</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nature. 2006 Jun 29;441(7097):1162-6</RefSource>
<PMID Version="1">16672981</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nat Cell Biol. 2006 Aug;8(8):834-42</RefSource>
<PMID Version="1">16862145</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nature. 2012 Sep 20;489(7416):391-9</RefSource>
<PMID Version="1">22996553</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Hum Mol Genet. 2012 Nov 15;21(22):4888-903</RefSource>
<PMID Version="1">22872702</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Biochem Biophys Res Commun. 2012 Nov 9;428(1):197-202</RefSource>
<PMID Version="1">23068103</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 2012 Nov 23;287(48):40652-60</RefSource>
<PMID Version="1">23060438</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nucleic Acids Res. 2012 Dec;40(22):11583-93</RefSource>
<PMID Version="1">23042678</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Mol Cell. 2013 Mar 7;49(5):908-21</RefSource>
<PMID Version="1">23453807</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Science. 2013 Apr 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" MajorTopicYN="N">Mice</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008928" MajorTopicYN="N">Mitochondria</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
<QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D033681" MajorTopicYN="N">Mitochondrial Membrane Transport Proteins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D024101" MajorTopicYN="N">Mitochondrial Proteins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D063269" MajorTopicYN="N">Mitochondrial Turnover</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010300" MajorTopicYN="N">Parkinson Disease</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000503" MajorTopicYN="N">physiopathology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D051381" MajorTopicYN="N">Rats</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D044767" MajorTopicYN="N">Ubiquitin-Protein Ligases</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D054875" MajorTopicYN="N">Ubiquitination</DescriptorName>
</MeshHeading>
</MeshHeadingList>
<OtherID Source="NLM">PMC4563777 [Available on 10/01/16]</OtherID>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2013</Year>
<Month>10</Month>
<Day>29</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="revised"><Year>2014</Year>
<Month>10</Month>
<Day>08</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2014</Year>
<Month>11</Month>
<Day>25</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2015</Year>
<Month>1</Month>
<Day>17</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2015</Year>
<Month>1</Month>
<Day>17</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2016</Year>
<Month>6</Month>
<Day>15</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">25591737</ArticleId>
<ArticleId IdType="pii">cdd2014224</ArticleId>
<ArticleId IdType="doi">10.1038/cdd.2014.224</ArticleId>
<ArticleId IdType="pmc">PMC4563777</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Sante/explor/ParkinsonFranceV1/Data/PubMed/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000277 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd -nk 000277 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Wicri/Sante |area= ParkinsonFranceV1 |flux= PubMed |étape= Curation |type= RBID |clé= pubmed:25591737 |texte= Parkin maintains mitochondrial levels of the protective Parkinson's disease-related enzyme 17-β hydroxysteroid dehydrogenase type 10. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Curation/RBID.i -Sk "pubmed:25591737" \ | HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd \ | NlmPubMed2Wicri -a ParkinsonFranceV1
![]() | This area was generated with Dilib version V0.6.29. | ![]() |