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

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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.