Synaptojanin 1 Mutation in Parkinson's Disease Brings Further Insight into the Neuropathological Mechanisms
Identifieur interne : 000837 ( Main/Curation ); précédent : 000836; suivant : 000838Synaptojanin 1 Mutation in Parkinson's Disease Brings Further Insight into the Neuropathological Mechanisms
Auteurs : Valérie Drouet [France] ; Suzanne Lesage [France]Source :
- BioMed Research International [ 2314-6133 ] ; 2014.
English descriptors
- KwdEn :
- Base Sequence, Brain (physiopathology), Genetic Markers (genetics), Genetic Predisposition to Disease (epidemiology), Genetic Predisposition to Disease (genetics), Humans, Molecular Sequence Data, Mutation (genetics), Parkinson Disease (physiopathology), Phosphoric Monoester Hydrolases (genetics), Polymorphism, Single Nucleotide (genetics), Prevalence.
- MESH :
- chemical , genetics : Genetic Markers, Phosphoric Monoester Hydrolases.
- epidemiology : Genetic Predisposition to Disease.
- genetics : Genetic Predisposition to Disease, Mutation, Polymorphism, Single Nucleotide.
- physiopathology : Brain, Parkinson Disease.
- Base Sequence, Humans, Molecular Sequence Data, Prevalence.
Abstract
Synaptojanin 1 (SYNJ1) is a phosphoinositide phosphatase highly expressed in nerve terminals. Its two phosphatase domains dephosphorylate phosphoinositides present in membranes, while its proline-rich domain directs protein-protein interactions with synaptic components, leading to efficient recycling of synaptic vesicles in neurons. Triplication of SYNJ1 in Down's syndrome is responsible for higher level of phosphoinositides, enlarged endosomes, and learning deficits. SYNJ1 downregulation in Alzheimer's disease models is protective towards amyloid-beta peptide (A
Url:
DOI: 10.1155/2014/289728
PubMed: 25302295
PubMed Central: 4181773
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PMC:4181773Le document en format XML
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type="wicri:Area/Main/Curation">000837</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Synaptojanin 1 Mutation in Parkinson's Disease Brings Further Insight into the Neuropathological Mechanisms</title><author><name sortKey="Drouet, Valerie" sort="Drouet, Valerie" uniqKey="Drouet V" first="Valérie" last="Drouet">Valérie Drouet</name><affiliation wicri:level="3"><nlm:aff id="I1">Sorbonne Universités, UPMC (Paris 6), UMR S 1127, Inserm U 1127, CNRS UMR 7225, and ICM, 75013 Paris, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>Sorbonne Universités, UPMC (Paris 6), UMR S 1127, Inserm U 1127, CNRS UMR 7225, and ICM, 75013 Paris</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Paris</settlement></placeName></affiliation><affiliation wicri:level="3"><nlm:aff id="I2">Hôpital Pitié-Salpêtrière, Institut du Cerveau et de la Moelle Epinière ICM, 4ème Étage, 47 Boulevard de l'Hôpital, 75651 Paris, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>Hôpital Pitié-Salpêtrière, Institut du Cerveau et de la Moelle Epinière ICM, 4ème Étage, 47 Boulevard de l'Hôpital, 75651 Paris</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Paris</settlement></placeName></affiliation></author><author><name sortKey="Lesage, Suzanne" sort="Lesage, Suzanne" uniqKey="Lesage S" first="Suzanne" last="Lesage">Suzanne Lesage</name><affiliation wicri:level="3"><nlm:aff id="I1">Sorbonne Universités, UPMC (Paris 6), UMR S 1127, Inserm U 1127, CNRS UMR 7225, and ICM, 75013 Paris, France</nlm:aff><country xml:lang="fr">France</country><wicri:regionArea>Sorbonne Universités, UPMC (Paris 6), UMR S 1127, Inserm U 1127, CNRS UMR 7225, and ICM, 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">BioMed Research International</title><idno type="ISSN">2314-6133</idno><idno type="eISSN">2314-6141</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Base Sequence</term><term>Brain (physiopathology)</term><term>Genetic Markers (genetics)</term><term>Genetic Predisposition to Disease (epidemiology)</term><term>Genetic Predisposition to Disease (genetics)</term><term>Humans</term><term>Molecular Sequence Data</term><term>Mutation (genetics)</term><term>Parkinson Disease (physiopathology)</term><term>Phosphoric Monoester Hydrolases (genetics)</term><term>Polymorphism, Single Nucleotide (genetics)</term><term>Prevalence</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Genetic Markers</term><term>Phosphoric Monoester Hydrolases</term></keywords><keywords scheme="MESH" qualifier="epidemiology" xml:lang="en"><term>Genetic Predisposition to Disease</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Genetic Predisposition to Disease</term><term>Mutation</term><term>Polymorphism, Single Nucleotide</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>Base Sequence</term><term>Humans</term><term>Molecular Sequence Data</term><term>Prevalence</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Synaptojanin 1 (SYNJ1) is a phosphoinositide phosphatase highly expressed in nerve terminals. Its two phosphatase domains dephosphorylate phosphoinositides present in membranes, while its proline-rich domain directs protein-protein interactions with synaptic components, leading to efficient recycling of synaptic vesicles in neurons. Triplication of SYNJ1 in Down's syndrome is responsible for higher level of phosphoinositides, enlarged endosomes, and learning deficits. SYNJ1 downregulation in Alzheimer's disease models is protective towards amyloid-beta peptide (A<italic>β</italic>) toxicity. One missense mutation in one of SYNJ1 functional domains was recently incriminated in an autosomal recessive form of early-onset Parkinson's disease (PD). In the third decade of life, these patients develop progressive Parkinsonism with bradykinesia, dystonia, and variable atypical symptoms such as cognitive decline, seizures, and eyelid apraxia. The identification of this new gene, together with the fact that most of the known PD proteins play a role in synaptic vesicle recycling and lipid metabolism, points out that synaptic maintenance is a key player in PD pathological mechanisms. Studying PD genes as a network regulating synaptic activity could bring insight into understanding the neuropathological processes of PD and help identify new genes at fault in this devastating disorder.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Mcpherson, Ps" uniqKey="Mcpherson P">PS Mcpherson</name></author><author><name sortKey="Czernik, Aj" uniqKey="Czernik A">AJ Czernik</name></author><author><name sortKey="Chilcote, Tj" uniqKey="Chilcote T">TJ Chilcote</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Mcpherson, Ps" uniqKey="Mcpherson P">PS McPherson</name></author><author><name sortKey="Takei, K" uniqKey="Takei K">K Takei</name></author><author><name sortKey="Schmid, Sl" uniqKey="Schmid S">SL Schmid</name></author><author><name sortKey="De Camilli, P" uniqKey="De Camilli P">P de Camilli</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Krebs, Ce" 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