Effect of homodimerization of G-protein coupled receptors on the cell signaling and the affinity to ligands
| Project/Area Number |
21590273
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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 |
General pharmacology
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| Research Institution | University of Fukui |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
MURAMATSU Ikunobu 福井大学, 医学部, 教授 (10111965)
SUZUKI Fumiko 福井大学, 医学部, 助教 (80291376)
NISHIMUNE Atsushi 福井大学, 医学部, 助教 (40311310)
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| Project Period (FY) |
2009 – 2011
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| Project Status |
Completed (Fiscal Year 2011)
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| Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2011: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000)
Fiscal Year 2010: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2009: ¥3,120,000 (Direct Cost: ¥2,400,000、Indirect Cost: ¥720,000)
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| Keywords | 受容体 / チャネル / 輸送系 / シグナル情報伝達系 / ダイマー / カルシウム |
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| Research Abstract |
Functional G-protein coupled receptors are believed to be functional when dimerized. Still, in the receptor dimer, each subunit(one receptor molecule) binds to one agonist, respectively. When coexpressed with Snapin, which intereacts with alpha-1A receptors, Sanpin also dimerizes, and each Snapin can bind to the receptor. Thus, alpha-1A receptor can also form dimmer. Interestingly, the receptor dimer with Snapin can bin only to one agonist, suggesting that the functional dimmer when coexisted with Snapin may form a different structure from the dimmer without Snapin.
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Report
(4 results)
Research Products
(29 results)
