Structural analysis of cytoskeletal regulatory protein
| Project/Area Number |
20770093
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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 |
Structural biochemistry
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| Research Institution | The Institute of Physical and Chemical Research |
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Principal Investigator |
SUETSUGU Kyoko The Institute of Physical and Chemical Research, システム研究チーム, 研究員 (40391990)
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| Project Period (FY) |
2008 – 2009
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| Project Status |
Completed (Fiscal Year 2009)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2009: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2008: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | 細胞骨格 / X線構造解析 / 細胞膜 / タンパク質 / シグナル伝達 / 低分子Gタンパク質 / アクチン / X線結晶構造解析 / 細胞運動 |
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| Research Abstract |
We solved the crystal structures of N-WASP binding protein ; EFCLpacsin2 (residues 1-343 ; EFC/F-BAR domain + C-terminal extension) and EFCSpacsin2 (residues1-305 ; EFC/F-BAR domain) at 2.7 and 2.0 A resolutions, respectively. We found that overexpression of the pacsin2 EFC/F-BAR domain induced cellular microspikes, with the pacsin2 EFC/F-BAR domain concentrated at the neck. The hydrophobic loops and the basic amino-acid residues on the concave surface of the pacsin2 EFC/F-BAR domain are essential for both the microspike formation and tubulation. Since the curvature of the neck of the microspike and that of the tubulation share similar geometry, the pacsin2 EFC/FBAR domain is considered to facilitate both microspike formation and tubulation.
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Report
(3 results)
Research Products
(3 results)
