Project/Area Number |
04304057
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Research Category |
Grant-in-Aid for Co-operative Research (A)
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Allocation Type | Single-year Grants |
Research Field |
分子遺伝学・分子生理学
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Research Institution | UNIVERSITY OF TOKYO |
Principal Investigator |
MABUCHI Issei Univ.of Tokyo, Coll.Arts & Sci.Professor, 教養学部, 教授 (40012520)
|
Co-Investigator(Kenkyū-buntansha) |
HISANAGA Shin-ichi Tokyo Inst.Technol., Fac.Life Sci.Assoc.Professor, 生命理工学部, 助教授 (20181092)
NOUMURA Taiko Ochanomizu Womens Univ., Fac.Sci.Professor, 理学部, 教授 (30022578)
HAMAGUCHI Yukihisa Tokyo Inst.Technol., Fac.Sci.Professor, 理学部, 教授 (70016161)
HOTANI Hirokazu Nagoya Univ., Fac.Sci.Professor, 理学部, 教授 (80025444)
FUJII Ryuzo Toho Univ., Fac.Sci.Professor, 理学部, 教授 (10045354)
月田 承一郎 岡崎国立共同研究機構生理学研究所, 教授 (50155347)
|
Project Period (FY) |
1992 – 1993
|
Project Status |
Completed (Fiscal Year 1993)
|
Budget Amount *help |
¥13,000,000 (Direct Cost: ¥13,000,000)
Fiscal Year 1993: ¥6,000,000 (Direct Cost: ¥6,000,000)
Fiscal Year 1992: ¥7,000,000 (Direct Cost: ¥7,000,000)
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Keywords | Cytokinesis / Action filaments / Microtubules / Intermediate filaments / Contractile ring / Mitotic apparatus / Dynein / Kinesin / 細胞接着装置 / ミオシン / リン酸化 |
Research Abstract |
1) Cytokinesis : It has been shown that both protein phosphorylation and a low molecular weight protein rho are involved in the organization of the contractile ring. 2) In vitro motility : Tropomyosin-troponin enhances efficiency of chemical-mechanical energy transfomation in the actomyosin interaction. Kinesin head domain has been shown to be able to slide microtubules (MTs). 3) Structure-function relationship of actin : Chimera actins have been produced from Tetrahymena and Dictyostelium. A segment spanning from res. 38-83 in the actin sequence has been shown to interact with DNase I.4) Membrance-skeleton interaction : ERM family proteins are involved in constitution of the actin cytoskeleton. These proteins directly interact with the membrane protein CD44.5) Mitotic apparatus : Hexylene glycol, a MT-stabilizer, enlarges metaphase spindle at concentrations less than 3%, and slows chromosome movements. 6) Motility in chromatophores : Ca ion concentration raises prior to aggregation of pigments in melanophores. Pigments moves through interaction between motor proteins and MTs. 7) Brain MTs : An epitope for anti-tubulin antibody E3B8 is present in res. 432-452 which is common in all alpha-tubulins. 8) Dynamic properties of MTs : MTs switch from depolymerization phase to polymerization phase at the site of MAPs binding. The MT-satsbilizing ability of MAPs is abolished by phosphorylation by MPF.22S dynein binds to MTs in an ATP-sensitive manner and thereby stabilizes the MTs. 9) Intermediate filaments : Type 2A phosphatase associates with neurofilaments in the spinal cord and stabilizes the neurofilaments. It ia likely that CaM-kinase II is a intermediate filament-kinase during cell division.
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