The endoplasmic reticulum/mitochondria interface: a subcellular platform for the orchestration of the functions of the PINK1-Parkin pathway?
Identifieur interne : 000476 ( Main/Exploration ); précédent : 000475; suivant : 000477The endoplasmic reticulum/mitochondria interface: a subcellular platform for the orchestration of the functions of the PINK1-Parkin pathway?
Auteurs : Zoi Erpapazoglou [France] ; Olga Corti [France]Source :
- Biochemical Society transactions [ 1470-8752 ] ; 2015.
English descriptors
- KwdEn :
- Animals, Endoplasmic Reticulum (metabolism), Endoplasmic Reticulum (pathology), Humans, Mitochondria (genetics), Mitochondria (metabolism), Mitochondria (pathology), Mutation, Nerve Degeneration (genetics), Nerve Degeneration (metabolism), Parkinson Disease (genetics), Parkinson Disease (metabolism), Parkinson Disease (pathology), Protein Kinases (genetics), Protein Kinases (metabolism), Signal Transduction, Ubiquitin-Protein Ligases (genetics), Ubiquitin-Protein Ligases (metabolism).
- MESH :
- chemical , genetics : Protein Kinases, Ubiquitin-Protein Ligases.
- genetics : Mitochondria, Nerve Degeneration, Parkinson Disease.
- metabolism : Endoplasmic Reticulum, Mitochondria, Nerve Degeneration, Parkinson Disease, Protein Kinases, Ubiquitin-Protein Ligases.
- pathology : Endoplasmic Reticulum, Mitochondria, Parkinson Disease.
- Animals, Humans, Mutation, Signal Transduction.
Abstract
Mitochondrial dysfunction is a hallmark of both idiopathic and familial Parkinson's disease (PD). Mutations in the PARK2 and PARK6 genes, coding for the cytosolic E3 ubiquitin protein ligase Parkin and the mitochondrial serine/threonine kinase PINK1 [phosphatase and tensin homologue (PTEN)-induced putative kinase 1], lead to clinically similar early-onset Parkinsonian syndromes. PINK1 and Parkin cooperate within a conserved pathway to preserve mitochondrial quality through the regulation of a variety of processes, including mitochondrial dynamics, transport, bioenergetics, biogenesis and turnover. The molecular mechanisms behind the orchestration of this plethora of functions remain poorly understood. In the present review, we emphasize the functional overlap between the PINK1-Parkin pathway and the endoplasmic reticulum (ER)-mitochondria interface, a subcellular compartment critically involved in neurodegeneration. We discuss how this compartment may constitute a hub for the spatiotemporal organization of the activities of the PINK1-Parkin pathway.
DOI: 10.1042/BST20150008
PubMed: 25849933
Affiliations:
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santé et de la recherche médicale, Inserm, U1127, F-75013, Paris</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Paris</settlement></placeName></affiliation></author><author><name sortKey="Corti, Olga" sort="Corti, Olga" uniqKey="Corti O" first="Olga" last="Corti">Olga Corti</name><affiliation wicri:level="3"><nlm:affiliation>*Institut national de la santé et de la recherche médicale, Inserm, U1127, F-75013, Paris, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>*Institut national de la santé et de la recherche médicale, Inserm, U1127, F-75013, Paris</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Paris</settlement></placeName></affiliation></author></analytic><series><title level="j">Biochemical Society transactions</title><idno type="eISSN">1470-8752</idno><imprint><date when="2015" 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Ligases</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Mitochondria</term><term>Nerve Degeneration</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Endoplasmic Reticulum</term><term>Mitochondria</term><term>Nerve Degeneration</term><term>Parkinson Disease</term><term>Protein Kinases</term><term>Ubiquitin-Protein Ligases</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Endoplasmic Reticulum</term><term>Mitochondria</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Humans</term><term>Mutation</term><term>Signal Transduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Mitochondrial dysfunction is a hallmark of both idiopathic and familial Parkinson's disease (PD). Mutations in the PARK2 and PARK6 genes, coding for the cytosolic E3 ubiquitin protein ligase Parkin and the mitochondrial serine/threonine kinase PINK1 [phosphatase and tensin homologue (PTEN)-induced putative kinase 1], lead to clinically similar early-onset Parkinsonian syndromes. PINK1 and Parkin cooperate within a conserved pathway to preserve mitochondrial quality through the regulation of a variety of processes, including mitochondrial dynamics, transport, bioenergetics, biogenesis and turnover. The molecular mechanisms behind the orchestration of this plethora of functions remain poorly understood. In the present review, we emphasize the functional overlap between the PINK1-Parkin pathway and the endoplasmic reticulum (ER)-mitochondria interface, a subcellular compartment critically involved in neurodegeneration. We discuss how this compartment may constitute a hub for the spatiotemporal organization of the activities of the PINK1-Parkin pathway.</div></front></TEI><affiliations><list><country><li>France</li></country><region><li>Île-de-France</li></region><settlement><li>Paris</li></settlement></list><tree><country name="France"><region name="Île-de-France"><name sortKey="Erpapazoglou, Zoi" sort="Erpapazoglou, Zoi" uniqKey="Erpapazoglou Z" first="Zoi" last="Erpapazoglou">Zoi Erpapazoglou</name></region><name sortKey="Corti, Olga" sort="Corti, Olga" uniqKey="Corti O" first="Olga" last="Corti">Olga Corti</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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