Schizophrenia susceptibility gene product dysbindin-1 regulates the homeostasis of cyclin D1

被引:8
作者
Ito, Hidenori [1 ]
Morishita, Rika [1 ]
Nagata, Koh-ichi [1 ,2 ]
机构
[1] Aichi Human Serv Ctr, Inst Dev Res, Dept Mol Neurobiol, 713-8 Kamiya, Kasugai, Aichi 4800392, Japan
[2] Nagoya Univ, Grad Sch Med, Dept Neurochem, Nagoya, Aichi 4648601, Japan
来源
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE | 2016年 / 1862卷 / 08期
关键词
Dysbindin-1; Cyclin D1; Schizophrenia; NUCLEAR EXPORT SIGNAL; PREFRONTAL CORTEX; DEPENDENT KINASE; BINDING PARTNER; PROTEIN; DTNBP1; COMPLEX; MICE; DOPAMINE; MUTANT;
D O I
10.1016/j.bbadis.2016.04.016
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Dysbindin-1 (dystrobrevin binding protein-1, DTNBP1) is now widely accepted as a potential schizophrenia susceptibility gene and accumulating evidence indicates its functions in the neural development. In this study, we tried to identify new binding partners for dysbindin-1 to clarify the novel function of this molecule. When consulted with BioGRID protein interaction database, cyclin D3 was found to be a possible binding partner for dysbindin-1. We then examined the interaction between various dysbindin-1 isoforms (dysbindin-1A, -1B and -1C) and all three D-type cyclins (cyclin D1, D2, and D3) by immunoprecipitation with the COS7 cell expression system, and found that dysbindin-1A preferentially interacts with cyclin D1. The mode of interaction between these molecules was considered as direct binding since recombinant dysbindin-1A and cyclin D1 formed a complex in vitro. Mapping analyses revealed that the C-terminal region of dysbindin-1A binds to the C-terminal of cyclin D1. Consistent with the results of the biochemical analyses, endogenous dysbindin-1 was partially colocalized with cyclin D1 in NIH3T3 fibroblast cells and in neuronal stem and/or progenitor cells in embryonic mouse brain. While co-expression of dysbindin-1A with cyclin D1 changed the localization of the latter from the nucleus to cytosol, cyclin D1-binding partner CDK4 inhibited the dysbindin-cyclin D1 interaction. Meanwhile, depletion of endogenous dysbindin-1A increased cyclin D1 expression. These results indicate that dysbindin-1A may control the cyclin D1 function spatiotemporally and might contribute to better understanding of the pathophysiology of dysbindin-1-associated disorders. (C) 2016 Elsevier B.V. All rights reserved.
引用
收藏
页码:1383 / 1391
页数:9
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