First Author | Soma M | Year | 2014 |
Journal | Neurosci Lett | Volume | 582 |
Pages | 120-4 | PubMed ID | 25196196 |
Mgi Jnum | J:215546 | Mgi Id | MGI:5605610 |
Doi | 10.1016/j.neulet.2014.08.046 | Citation | Soma M, et al. (2014) Dysbindin-1, a schizophrenia-related protein, interacts with HDAC3. Neurosci Lett 582:120-4 |
abstractText | DTNBP1 is a key candidate gene associated with schizophrenia. The expression of its protein product, dysbindin-1, is altered in the brains of schizophrenic patients; however, the physiological functions of dysbindin-1 in the central nervous system are unclear. Several studies have shown that both dysbindin-1 and histone deacetylase 3 (HDAC3) can be phosphorylated by the DNA-dependent protein kinase complex. In this study, we investigated the relationship between dysbindin-1 and HDAC3. We found that dysbindin-1 formed a protein complex with HDAC3 in human neuroblastoma cells and in mouse brain. The interaction between dysbindin-1 and HDAC3 occurred in an isoform-specific manner: HDAC3 coupled with dysbindin-1A and -1B, but not -1C. We also found that dysbindin-1B expression was increased in the nucleus in the presence of HDAC3, and, conversely, that the phosphorylation level of HDAC3 increased in the presence of dysbindin-1B. Taken together, these results identify a novel binding partner for dysbindin-1, which may potentially provide a new avenue for research into the neurological mechanisms of schizophrenia. |