Mints, Munc18-interacting proteins in synaptic vesicle exocytosis
Mints, Munc18-interacting proteins in synaptic vesicle exocytosis
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DOI：
10.1074/jbc.272.50.31459
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发表时间：
1997-12-12
影响因子：
4.8
通讯作者：
Sudhof, TC
中科院分区：
文献类型：
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作者：
Okamoto, M;Sudhof, TC
Munc18-1是一种与syntaxin 1相互作用的神经元蛋白，是突触囊泡胞吐所必需的。我们现在已经确定了两个称为Mint1和Mint2的Munc18-1相互作用蛋白，它们可能介导Munc18-1的功能。薄荷蛋白仅在大脑中可检测到，由一个结合Munc18-1的n端序列（一个中间磷酸酪氨酸结合域）和两个被认为将蛋白质附着在质膜上的c端PDZ结构域组成。在大脑中，薄荷蛋白是含有Munc18-1和syntaxin的多聚体复合体的一部分，可能在突触囊泡对接/融合中起中间作用。磷脂酪氨酸结合区域特异性结合磷脂酰肌醇磷酸，已知在囊泡胞出过程中产生（Hay， J. C., Fisette， P. L., Jenkins， G. H., Fukami， K., Takonawa， T., Anderson， R. A.和Martin， T. F. J. (1995) Nature 374, 173-177）。我们的数据提出了一种模型，即局部生产的磷脂酰肌醇磷酸可能触发囊泡通过Minc与活性区结合。Munc18-1复合物与syntaxin 1结合。
Munc18-1 is a neuronal protein that interacts with syntaxin 1 and is required for synaptic vesicle exocytosis. We have now identified two Munc18-1-interacting proteins called Mint1 and Mint2 that may mediate the function of Munc18-1. Mint proteins are detectable only in brain and are composed of an N-terminal sequence that binds Munc18-1, a middle phosphotyrosine-binding domain, and two C-terminal PDZ domains thought to attach proteins to the plasma membrane. In brain, Mint proteins are part of a multimeric complex containing Munc18-1 and syntaxin that likely functions as an intermediate in synaptic vesicle docking/fusion. The phosphotyrosine-binding domain specifically binds to phosphatidylinositol phosphates known to be produced during vesicle exocytosis (Hay, J. C., Fisette, P. L., Jenkins, G. H., Fukami, K., Takonawa, T., Anderson, R. A., and Martin, T. F. J. (1995) Nature 374, 173-177). Our data suggest a model whereby local production of phosphatidylinositol phosphates may trigger the binding of vesicles to the active zone via the Minc.Munc18-1 complex in conjunction with syntaxin 1.