2002 Fiscal Year Final Research Report Summary
The study for the function of synapsins in Synaptic vesicles and secretory granules
| Project/Area Number |
13680837
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Neurochemistry/Neuropharmacology
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| Research Institution | Gunma University |
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Principal Investigator |
HOSAKA Masahiro Department of Melecular Medicine, Institute for Molecular and Cellular Regulation, Gunma University, Assistant Professor, 生体調節研究所, 講師 (80311603)
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| Project Period (FY) |
2001 – 2002
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| Keywords | Synapsin / Synaptic Vesicles / Chromogranin A / Secretogranin III / ATPase / Secretory Granules |
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| Research Abstract |
A project of Synapsin in Synaptic vesicles
Synapsins 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 Cells
Chromogranin 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.
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