2013 Fiscal Year Final Research Report
Function of tubulin polyglutamylation in cilia/flagella motility mechanism
Project/Area Number |
23570189
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Biophysics
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Research Institution | Gakushuin University (2012-2013) The University of Tokyo (2011) |
Principal Investigator |
KAMIYA Ritsu 学習院大学, 理学部, 客員教授 (10124314)
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Project Period (FY) |
2011 – 2013
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Keywords | 運動・輸送 / 分子モーター / 翻訳後修飾 / 鞭毛・繊毛 / 微小管 |
Research Abstract |
To approach the function of tubulin polyglutamylation in cilia/flagella motility, we examined the motile properties of a Chlamydomonas tpg1, a mutant that lacks a tubulin polygultamylating enzyme (TTLL9). Motility analyses in double mutants between tpg1 and various kinds of dynein-deficient mutants revealed that long-chain tubulin polyglutamylation affects the function of only one particular species of dynein, inner arm dynein e, among more than 10 species of axonemal dyneins. Furthermore, studies using another mutant, tpg2, showed that a protein designated FAP234 functions in the transport and stabilization of TTLL9.
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Research Products
(8 results)
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[Journal Article] The MIA complex is a conserved and novel dynein regulator essential for normal ciliary motility2013
Author(s)
Yamamoto, R., Song, K., Yanagisawa, H., Fox, L., Yagi, T., Wirschell, M., Hirono, M., Kamiya, R., Nicastro, D., and Sale, W.S.
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Journal Title
J. Cell Biol.
Volume: 201
Pages: 263-278
DOI
Peer Reviewed
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