Source:http://linkedlifedata.com/resource/pubmed/id/19573021
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2009-9-2
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pubmed:abstractText |
Schizophrenia is a complex mental disorder with fairly high level of heritability. Dystrobrevin binding protein 1, a gene encoding dysbindin protein, is a susceptibility gene for schizophrenia that was identified by family-based association analysis. Recent studies revealed that dysbindin is involved in the exocytosis and/or formation of synaptic vesicles. However, the molecular function of dysbindin in synaptic transmission is largely unknown. To investigate the signaling pathway in which dysbindin is involved, we isolated dysbindin-interacting molecules from rat brain lysate by combining ammonium sulfate precipitation and dysbindin-affinity column chromatography, and identified dysbindin-interacting proteins by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and liquid chromatography-tandem mass spectrometry. Proteins involved in protein localization process, including Munc18-1, were identified as dysbindin-interacting proteins. Munc18-1 was co-immunoprecipitated with dysbindin from rat brain lysate, and directly interacted with dysbindin in vitro. In primary cultured rat hippocampal neurons, a part of dysbindin was co-localized with Munc18-1 at pre-synaptic terminals. Our result suggests a role for dysbindin in synaptic vesicle exocytosis via interaction with Munc18-1.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1471-4159
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pubmed:author |
pubmed-author:FujinoYasutakaY,
pubmed-author:FunahashiYusukeY,
pubmed-author:HashimotoRyotaR,
pubmed-author:HikitaTakaoT,
pubmed-author:KaibuchiKozoK,
pubmed-author:KurodaKeisukeK,
pubmed-author:OhtaKanaeK,
pubmed-author:ShinodaTomoyasuT,
pubmed-author:Taneichi-KurodaSetsukoS,
pubmed-author:TayaShinichiroS,
pubmed-author:TsuboiDaisukeD,
pubmed-author:Uraguchi-AsakiJunkoJ
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pubmed:issnType |
Electronic
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pubmed:volume |
110
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1567-74
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pubmed:meshHeading |
pubmed-meshheading:19573021-Animals,
pubmed-meshheading:19573021-Carrier Proteins,
pubmed-meshheading:19573021-Exocytosis,
pubmed-meshheading:19573021-Hippocampus,
pubmed-meshheading:19573021-Humans,
pubmed-meshheading:19573021-Mice,
pubmed-meshheading:19573021-Mice, Inbred C57BL,
pubmed-meshheading:19573021-Munc18 Proteins,
pubmed-meshheading:19573021-Protein Binding,
pubmed-meshheading:19573021-Proteomics,
pubmed-meshheading:19573021-Rats,
pubmed-meshheading:19573021-Schizophrenia
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pubmed:year |
2009
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pubmed:articleTitle |
Proteomic analysis reveals novel binding partners of dysbindin, a schizophrenia-related protein.
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pubmed:affiliation |
Department of Cell Pharmacology, Graduate School of Medicine, Nagoya University, Nagoya, Aichi 466-8550, Japan.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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