| First Author | Hikita T | Year | 2009 |
| Journal | J Neurochem | Volume | 110 |
| Issue | 5 | Pages | 1567-74 |
| PubMed ID | 19573021 | Mgi Jnum | J:152240 |
| Mgi Id | MGI:4357717 | Doi | 10.1111/j.1471-4159.2009.06257.x |
| Citation | Hikita T, et al. (2009) Proteomic analysis reveals novel binding partners of dysbindin, a schizophrenia-related protein. J Neurochem 110(5):1567-74 |
| 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. |
