| Project/Area Number |
22790182
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
General anatomy (including Histology/Embryology)
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| Research Institution | Tokyo Medical and Dental University |
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Principal Investigator |
HOSHINO Mitsunobu 東京医科歯科大学, 大学院・医歯学総合研究科, 助教 (60431962)
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| Research Collaborator |
TERADA Sumio 東京医科歯科大学, 医歯学総合研究科, 教授 (00262022)
KAWAGISHI Masahiko 東京医科歯科大学, 医歯学総合研究科, 助教 (60323606)
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| Project Period (FY) |
2010 – 2011
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| Project Status |
Completed (Fiscal Year 2011)
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| Budget Amount *help |
¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2011: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2010: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
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| Keywords | 神経細胞生物学 / 分子形態学 / Ras / 低分子量GTP結合タンパク質 / Rig / 膜輸送 / 神経細胞 / 低子量GTP結合タンパク質 |
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| Research Abstract |
The newly discovered Ras-like small GTPase protein Rig is expressed prominently in neural cells and has a C-terminal CAAX prenylation motif required for membrane association. Although Rig shares high sequence identity with Ras, its physiological functions in neural cells have remained to be clarified. We have found that overexpressed Rig protein was colocalized with transferrin and with Rab11, a marker protein of recycling endosomes. Although the recycling kinetics of transferrin seemed to be indifferent to overexpressed either GTP or GDP-bound Rig mutant protein, the prenylation-deficient Rig mutant protein induced slowing down of the recycling kinetics. When this prenylation-deficient mutant protein was overexpressed in primary-cultured mouse hippocampal neurons, dendrites had fewer arborizations than those of wild type protein-expressed cells. Furthermore, we have identified binding partner candidates of Rig protein by pull down methods to clarify the physiological roles of Rig protein, such as the regulation of recycling membrane traffics and the cellular morphogenesis of neural cells.
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