| Project/Area Number |
10213101
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| Research Category |
Grant-in-Aid for Scientific Research on Priority Areas
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| Allocation Type | Single-year Grants |
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| Review Section |
Biological Sciences
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| Research Institution | The University of Tokyo |
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Principal Investigator |
MABUCHI Issei The University of Tokyo, Graduate School of Arts and Sciences, Professor, 大学院・総合文化研究科, 教授 (40012520)
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| Co-Investigator(Kenkyū-buntansha) |
HOSOYA Hiroshi Hiroshima Universty, Graduate School of Science, Professor, 大学院・理学研究科, 教授 (90183102)
NUMATA Osamu The University of Tsukuba, Institute of Biological Sciences, Professor, 生物科学系, 教授 (50189354)
HAMAGUCHI Yukihisa Tokyo Institute of Technology, Graduate School of Bioscience and Biotechnology, Professor, 大学院・生命理工学研究科, 教授 (70016161)
TANAKA Kazuma Hokkaido University, Institute for Genetic Medicine, Professor, 遺伝子病制御研究所, 教授 (60188290)
KITAYAMA Hitoshi Kyoto University, Graduate School of Medicine, Associate Professor, 大学院・医学研究科, 助教授 (30231286)
渡辺 良雄 上武大学, 学長 (00015918)
丸山 工作 大学入試センター, 所長 (60012267)
石川 春律 群馬大学, 医学部, 教授 (90010058)
木下 専 京大院, 医学研究科, 助手 (30273460)
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| Project Period (FY) |
1998 – 2001
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| Project Status |
Completed (Fiscal Year 2002)
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| Budget Amount *help |
¥27,400,000 (Direct Cost: ¥27,400,000)
Fiscal Year 2002: ¥1,500,000 (Direct Cost: ¥1,500,000)
Fiscal Year 2001: ¥9,000,000 (Direct Cost: ¥9,000,000)
Fiscal Year 2000: ¥6,300,000 (Direct Cost: ¥6,300,000)
Fiscal Year 1999: ¥6,700,000 (Direct Cost: ¥6,700,000)
Fiscal Year 1998: ¥3,900,000 (Direct Cost: ¥3,900,000)
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| Keywords | cell, tissue / signal transduction / biomolecules / cell division / cytoskeleton / actin / myosin / contractile ring / 細胞組織 / 細胞質分裂 / 低分子量Gタンパク質 / アクチン調節タンパク質 / リン酸化 / 分裂溝 / 分裂シグナル / Rho / 微小管 / セプチン / PJ10 |
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| Research Abstract |
We analyzed mechanism of formation of the contractile ring using various cells. In fission yeast cells, the contractile ring is formed from F-actin cables which accumulate at the medial region of the cell during nuclear division. The aster-like structure consisting of F-actin cables and the leading cable which elongates from the structure are important in this process. Cdcl2 plays a role in elongation of the leading cable, while Cdc15 plays a role in the fusion of the F-actin cables to the leading cable. We also analyzed function of Rho proteins in fission yeast, and found a novel G-protein Rho3. Rho3 is localized to the cell membrane .It was found that a novel formin family protein For3 is present downstream of either Rho3 or Cdc42. Rho3 and For3 controls both actin cytoskeleton and microtubules, and thereby regulate shape of the cell and position of cytokinesis. Cla4(PAK) and Bni1 (formin) cooperatively function in regulation of the septin ring in budding yeast. F-actin plays an impo
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rtant role in this process. In Tetrahymena, dimeric EF1a bundles F-actin. Ca/calmodulin dissociates this EF1a dimer and thus inhibit the bundling of F-actin. Tetrahymena fimbrin binds and bundles F-actin in a Ca-insensitive manner. It is localized to the cleavage furrow. We found that actin is less concentrated in the cortex near the centrosome while concentrated in the cortex away from it, where the furrow is formed, in the fourth division in sea urchin embryos. Role of microtubules in formation of the contractile ring in Xenopus eggs was analyzed. Disruption of microtubules by microtubule poisons did not interfere with contraction of the contractile ring, but interfered with its formation. We also found that the microtubules emanated from the both poles link with each other beneath the cleavage furrow. We tested a possibility that Ca ions play a role in cleavage signaling by analyzing Ca release around the cleavage furrow. Neither Ca waves nor small Ca releases such as Ca puffs or Ca blips were found at the leading edge of the cleavage furrow. Rho-kinase in HeLa cells binds to filamin A. Thus, it is possible that these proteins co-localize in the contractile ring. Less
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