Structural basis for the ion channel anchoring of ankyrinG
| Project/Area Number |
24689012
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| Research Category |
Grant-in-Aid for Young Scientists (A)
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| Allocation Type | Partial Multi-year Fund |
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| Research Field |
General physiology
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| Research Institution | Osaka University |
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Principal Investigator |
FUJIWARA YUICHIRO 大阪大学, 医学(系)研究科(研究院), 准教授 (20532980)
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥26,910,000 (Direct Cost: ¥20,700,000、Indirect Cost: ¥6,210,000)
Fiscal Year 2013: ¥13,520,000 (Direct Cost: ¥10,400,000、Indirect Cost: ¥3,120,000)
Fiscal Year 2012: ¥13,390,000 (Direct Cost: ¥10,300,000、Indirect Cost: ¥3,090,000)
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| Keywords | 興奮収縮連関 / 跳躍伝導 / イオンチャネル / 構造機能連関 / パルミトイル化 / アンキリン / 軸索起始部 |
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| Outline of Final Research Achievements |
Ankyrin-G (AnkG) configures the membrane-excitation platform by clustering various ion channels in neurons and cardiomyocytes. AnkG itself localizes to the specific areas on the plasma membrane via the s-palmitoylation of Cys. However, the structural mechanism how AnkG anchors to the membrane is not understood. In this study, we solved the crystal structures of the s-palmitoylation domain of AnkG in reduced and oxidized forms of the Cys, and performed the long-term molecular dynamics simulation of the membrane association. Here we report that the s-palmitoylation facilitated the membrane anchoring of AnkG, defining a stable binding interface to the plasma membrane. AnkG without s-palmitoylation was apparently in contact with the membrane but did not have a unique binding interface. These suggest that AnkG is ready to accept the Cys modification in the juxtamembrane region, and, once it happens, constitutes the rigid structural base of the membrane-excitation platform.
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Report
(4 results)
Research Products
(32 results)
