The study for the function of synapsins in Synaptic vesicles and secretory granules

突触囊泡中突触蛋白的研究突触蛋白是一个调节神经递质释放的突触囊泡蛋白家族。在所有突触蛋白中只有两个结构域是保守的：一个短的N-末端A结构域，具有cAMP依赖性蛋白激酶（PKA）和CaM激酶I的单个磷酸化位点，以及一个大的中央C结构域，结合ATP并可能是酶。利用这项研究基金，我们试图证明突触蛋白的C结构域作为ATP酶工作，以及哪些未知底物与突触蛋白协同作用。为此，我们采用了酵母双杂交系统与大鼠cDNA文库。神经内分泌细胞分泌颗粒分选机制的研究嗜铬粒蛋白A（Chromogranin A，CgA）是神经内分泌细胞分泌颗粒中的一个重要蛋白质。由于CgA与分泌蛋白的结合倾向的属性可能是必不可少的，其分选分泌颗粒，我们筛选其结合伴侣蛋白使用酵母双杂交系统。作为结果，我们确定，SgIII结合到CgA和指导CgA分泌颗粒在各种内分泌细胞的特定相互作用。

A project of Synapsin in Synaptic vesiclesSynapsins constitute a family of synaptic vesicle proteins essential for regulating neurotransmitter release. Only two domains are conserved in all synapsins : a short N-terminal A domain with a single phosphorylation site for cAMP-dependent protein kinase (PKA) and CaM Kinase I, and a large central C domain that binds ATP and may be enzymatic. With this research grant, we tried to show that the C-domain of synapsins works as an ATPase and which unknown substrates co-laborate with synapsins. For these aims, we employed a yeast two-hybrid system with rat cDNA library. We are still analysing some candidate proteins.A project of Sorting Mechanisms to Secretory Granule in Neuroendocrine CellsChromogranin A (CgA) is transported restrictedly to regulated secretory granules in neuroendocrine cells. Because the binding-prone property of CgA with secretory proteins may be essential for its sorting to secretory granules, we screened its binding partner proteins using a yeast two-hybrid system. As results, we identified that SgIII binds to CgA and directs CgA to secretory granules by specific interactions in various endocrine cells.