Cooperation between multiple heads in moving dynein molecule
Project/Area Number |
20370057
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Research Category |
Grant-in-Aid for Scientific Research (B)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Biophysics
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Research Institution | The University of Tokyo |
Principal Investigator |
TOYOSHIMA Yoko The University of Tokyo, 大学院・総合文化研究科, 教授 (40158043)
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Co-Investigator(Renkei-kenkyūsha) |
EDAMATSU Masaki 東京大学, 大学院・総合文化研究科, 助教 (60251328)
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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 |
¥19,890,000 (Direct Cost: ¥15,300,000、Indirect Cost: ¥4,590,000)
Fiscal Year 2010: ¥3,510,000 (Direct Cost: ¥2,700,000、Indirect Cost: ¥810,000)
Fiscal Year 2009: ¥6,370,000 (Direct Cost: ¥4,900,000、Indirect Cost: ¥1,470,000)
Fiscal Year 2008: ¥10,010,000 (Direct Cost: ¥7,700,000、Indirect Cost: ¥2,310,000)
|
Keywords | ダイニン / 微小管 / 分子モーター / zincシート / プロセッシビティ / 歩行モデル / プロセッシビティー / 複数分子 / 分子間協同性 / ピンセット / 1分子計測 / 破断力 |
Research Abstract |
Cytoplasmic dynein is a two-headed microtubule (MT) motor protein. While kinesin moves by a hand-over-hand mechanism, the dynein walking mechanism is unknown. As the dynein motor domain is much larger than the step size, the two heads of dynein are thought to use multiple protofilaments of MT. Here we report dynein and kinesin motility on zinc-induced tubulin polymer (zinc-sheet), where only one protofilament can be used by motor proteins. Dynein and kinesin moved unidirectionally on a zinc-sheet at a similar velocity as MTs, demonstrating that both dynein and kinesin can walk on a single protofilament and multiple rows of parallel protofilaments are not essential for motility. These findings provide a clue as to how dynein uses the two huge motor domains for molecular walking.
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Report
(4 results)
Research Products
(49 results)
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[Journal Article] Inhibition of cytoplasmic dynein activity by CRMP-2 through a direct interaction.2009
Author(s)
Arimura, N., Hattori, A., Kimura, T., Nakamura, S., Funahashi, Y., Hirotsune, S., Furuta, K., Toyoshima, Y.Y., Kaibuchi, K.
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Journal Title
J Neurochem. 111
Pages: 380-390
Related Report
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[Journal Article] LIS1 and NDEL1 coordinate the plus-end-directed transport of cytoplasmic dynein.2008
Author(s)
Yamada, M.Toba, S., Yoshida, Y., Haratani, K., Mori, D., Yano, Y., Mimori-Kiyosue, Y., Nakamura, T., Ito,mK., Fushiki, S.,Setou, M., Whnshaw-Boris, A., Torisawa, T., Toyoshima, Y.Y., Hirotsune, S.
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Journal Title
EMBO J. 27
Pages: 2471-2483
Related Report
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[Journal Article] Direction and speed of microtubule movements driven by kinesin motors arranged on catchin thick filaments.2008
Author(s)
Taba, T., Edamatsu, M., Toba, S., Shibata, K., Imafuku, Y., Toyoshima, Y.Y., Tawada, K., Yamada, A.
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Journal Title
Cell Motility and the Cytoskeleton 65
Pages: 816-826
Related Report
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[Journal Article] The dynein stalk head, the microtubule binding-domain of dynein: NMR assignment and ligand binding.2008
Author(s)
Shimizu, Y., Kato, Y., Morii, H., Edamatsu, M., Toyoshima, Y.Y, Tanokura, M.
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Journal Title
J.Biomol.NMR 41
Pages: 89-96
Related Report
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[Journal Article] Direction and speed of microtubule movements driven by kinesin motorsarranged on catchin thick filaments2008
Author(s)
Taba, T., Edamatsu, M., Toba, S., Shibata, K, Imafuku, Y., Toyoshima, YY Tawada K and Yamada A
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Journal Title
Cell Motihty and the Cytoskeleton 65
Pages: 816-826
Related Report
Peer Reviewed
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