| Project/Area Number |
20570194
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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 |
Cell biology
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| Research Institution | National Cardiovascular Center Research Institute |
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Principal Investigator |
MASUDA Michitaka 独立行政法人国立循環器病研究センター, 細胞生物学部, 室長 (00190364)
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| Co-Investigator(Renkei-kenkyūsha) |
TAKEDA Soichi 独立行政法人国立循環器病研究センター, 心臓整理機能部, 室長 (80332279)
BEN Ammar Youssef 富士フイルム, 解析技術センター, 研究員 (90463273)
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| Project Period (FY) |
2008 – 2010
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| Project Status |
Completed (Fiscal Year 2010)
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| Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2010: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2009: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000)
Fiscal Year 2008: ¥2,860,000 (Direct Cost: ¥2,200,000、Indirect Cost: ¥660,000)
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| Keywords | 生体膜 / バードメイン / チロシンキナーゼ / タンパク質構造 / ナノバイオ / 生体分子 / BARドメイン |
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| Research Abstract |
Formation of tubes or buds from a flat membrane is a widely spread feature of the membrane shape change during the vesicular transport and the organelle morphogenesis. The BAR domain dimers exhibit curved banana shapes and appear to be suitable modules for this process. However, the BAR domains of Fer/Fes kinases, which have the coiled-coil domains just C-terminal of the BAR domain, show exceptionally low levels of membrane tubulation. We determined the crystal structure of the N-terminal half of Fer containing the BAR and the coiled-coil domains. They unite together into a banana-shape dimer. The membrane-binding surface of the dimer is not hindered by the coiled-coil domains. From comparison of the known BAR dimer structures, we have found out that there are two conserved residues on the non-membrane binding surfaces other than the Fer/Fes BAR domains. When these two residues of Fer were mutated into the conserved residues, the mutant Fer showed effective membrane tubulation activity. This result provides a new insight into the molecular mechanism for membrane deformation by the BAR domains.
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