| Project/Area Number |
23770119
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Structural biochemistry
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| Research Institution | Nara Institute of Science and Technology |
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Principal Investigator |
HIRANO Yoshinori 奈良先端科学技術大学院大学, バイオサイエンス研究科, 助教 (50452529)
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| Project Period (FY) |
2011 – 2012
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2012: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2011: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
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| Keywords | X線結晶構造解析 / 分子認識 / 積荷輸送 / ミオシン / 微小管 / 細胞内輸送 / 積荷認識 / 軸索ガイダンス / モータータンパク質 / 結晶構造解析 / 分子複合体 / 積み荷認識 |
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| Research Abstract |
The Cargo transportation by myosins is essential for proper cell phenomena. We peformed a series of structural and biochemicalstudies of the myosin-X tail domain , consisting of MyTH4 and FERM domains in complex with its specific cargo, a netrin receptor DCC (deleted in colorectal cancer). As the result, we found an unexpected binding mode of the DCC peptide, which is distinct from previously reported associations found in radixin/adhesion molecule complexes.
Moreover, we revealed direct interactions between the MyTH4-FERM domain and tubulin C-terminal acidic tails, and identified a positively charged patch of the MyTH4 domain as a tubulin binding region. We also demonstrated that both DCC and integrin bindings interfere with microtubule binding and that DCC binding interferes with integrin binding. Our results provide the molecular basis by which myosin-X facilitates alternative dual binding to cargos and microtubules.
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