2006 Fiscal Year Final Research Report Summary
A interacting protein specific to alpha-1 adrenoceptor modifies the receptor's function
| Project/Area Number |
17590215
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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 |
SUZUKI F. University of Fukui, Faculty of Medical sciences, Assistant Professor, 医学部, 助手 (80291376)
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| Co-Investigator(Kenkyū-buntansha) |
MORISHIMA S. University of Fukui, Faculty of Medical sciences, Senior Assistant Professor, 医学部, 講師 (50290911)
MURAMATSU I. University of Fukui, Faculty of Medical sciences, Professor, 医学部, 教授 (10111965)
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| Project Period (FY) |
2005 – 2006
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| Keywords | adrenoceptor / calcium channel / snapin |
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| Research Abstract |
Protein-to-protein interaction is one of the topics in receptor biology. We hypothesized that the α_<1A>-adrenoceptor (α_<1A>-AR) is accompanied with an interacting protein which modulates a receptor's function in native tissues. To isolate candidate proteins interacting with α_<1A>-AR, we searched human brain cDNA library by yeast two-hybrid method using the receptor as bait. As a result, Snapin, known as a binding partner of SNARE complex was identified. Snapin interacts and co-localizes with the α_<1A>-AR on plasma membrane of PC12 cells. Additionally, we found that the calcium entry upon α_<1A>-AR activation was significantly augmented when Snapin was co-expressed with the α_<1A>-AR in PC12 cells. On the other hand, Snapin interacts with TRPC6 channel which is now believed to be one of the receptor-operated calcium channels. Activation of the α_<1A>-AR induced the interaction between the receptor, increasing the recruitment of TRPC6 to the cell surface. Our data suggest a new receptor-operated signaling mechanism, where Snapin links the α_<1A>-AR to TRPC6, augmented calcium influx via receptor-operated calcium channels.
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