ArticleJournal of proteome research2014
Dysbindin-associated proteome in the p2 synaptosome fraction of mouse brain.
Article in Journal of proteome research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Genome-Wide Association Studies for Body Conformation Traits in Korean Holstein Population.Animals : an open access journal from MDPI · 2023Article
- Parvalbumin and Ubiquitin as Potential Biomarkers of Mercury Contamination of Amazonian Brazilian Fish.Biological trace element research · 2020Article
- The integrated landscape of causal genes and pathways in schizophrenia.Translational psychiatry · 2018Article
- Dysbindin-1 Involvement in the Etiology of Schizophrenia.International journal of molecular sciences · 2017Review
- Prevention of long-term memory loss after retrieval by an endogenous CaMKII inhibitor.Scientific reports · 2017Article
- Pallidin protein in neurodevelopment and its relation to the pathogenesis of schizophrenia.Molecular medicine reports · 2017Article
- Control of Hedgehog Signalling by the Cilia-Regulated Proteasome.Journal of developmental biology · 2016Review
- Cellular Protein WDR11 Interacts with Specific Herpes Simplex Virus Proteins at the trans-Golgi Network To Promote Virus Replication.Journal of virology · 2015Article
- T2D and Depression Risk Gene Proteasome Modulator 9 is Linked to Insomnia.Scientific reports · 2015Article
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Authors and funding
7 authors at 2 institutions in 1 country.
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Abstract
The gene DTNBP1 encodes the protein dysbindin and is among the most promising and highly investigated schizophrenia-risk genes. Accumulating evidence suggests that dysbindin plays an important role in the regulation of neuroplasticity. Dysbindin was reported to be a stable component of BLOC-1 complex in the cytosol. However, little is known about the endogenous dysbindin-containing complex in the brain synaptosome. In this study, we investigated the associated proteome of dysbindin in the P2 synaptosome fraction of mouse brain. Our data suggest that dysbindin has three isoforms associating with different complexes in the P2 fraction of mouse brain. To facilitate immunopurification, BAC transgenic mice expressing a tagged dysbindin were generated, and 47 putative dysbindin-associated proteins, including all components of BLOC-1, were identified by mass spectrometry in the dysbindin-containing complex purified from P2. The interactions of several selected candidates, including WDR11, FAM91A1, snapin, muted, pallidin, and two proteasome subunits, PSMD9 and PSMA4, were verified by coimmunoprecipitation. The specific proteasomal activity is significantly reduced in the P2 fraction of the brains of the dysbindin-null mutant (sandy) mice. Our data suggest that dysbindin is functionally interrelated to the ubiquitin-proteasome system and offer a molecular repertoire for future study of dysbindin functional networks in brain.
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