Elusidation of cartwheel-independent mechanisms for establishing 9-fold symmetry of the cdentriole structure
Project/Area Number |
24370079
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Research Category |
Grant-in-Aid for Scientific Research (B)
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Allocation Type | Partial Multi-year Fund |
Section | 一般 |
Research Field |
Cell biology
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Research Institution | Hosei University (2015) The University of Tokyo (2012-2014) |
Principal Investigator |
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Project Period (FY) |
2012-04-01 – 2016-03-31
|
Project Status |
Completed (Fiscal Year 2015)
|
Budget Amount *help |
¥16,900,000 (Direct Cost: ¥13,000,000、Indirect Cost: ¥3,900,000)
Fiscal Year 2014: ¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2013: ¥5,590,000 (Direct Cost: ¥4,300,000、Indirect Cost: ¥1,290,000)
Fiscal Year 2012: ¥7,280,000 (Direct Cost: ¥5,600,000、Indirect Cost: ¥1,680,000)
|
Keywords | 細胞骨格・運動 / 微小管 / 基底小体 / 繊毛 |
Outline of Final Research Achievements |
Centrioles are organelles with a cylindrical shape consisting of nine triplet microtubules. This 9-fold symmetrical structure is highly conserved among centrioles of most eukaryotic organisms. We previously reported that the cartwheel, a subcentriolar structure with 9-fold symmetry, largely contributes to establishment of the 9-fold symmetry of the centriole. In this study, we produced a cartwheel protein that assembles in vitro into cartwheel-like structures with 6-fold symmetry, and expressed it in Chlamydomonas cells. Observations of the centrioles and cartwheels in the cells suggested that a cartwheel-independent mechanism exists in the circular arrangement of the centriolar microtubules, and that a dynamic interaction between the mechanism and the cartwheel precisely determines the number of the triplets in the centriole.
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Report
(5 results)
Research Products
(24 results)
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[Journal Article] SAS-6 engineering reveals interdependence between cartwheel and microtubules in determining centriole architecture2016
Author(s)
Hilbert M*, Noga A*, Frey D*, Hamel V*, Guichard P, Kraatz SH, Pfreundschuh M, Hosner S, Flückiger I, Jaussi R, Wieser MM, Thieltges KM, Deupi X, Müller DJ, Kammerer RA, Gönczy P**, Hirono M**, Steinmetz MO**(**Corresponding authors)
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Journal Title
Nat Cell Biol
Volume: 18
Issue: 4
Pages: 393-403
DOI
Related Report
Peer Reviewed / Int'l Joint Research / Acknowledgement Compliant
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[Journal Article] FAP20 is an inner junction protein of doublet microtubules essential for both the planar asymmetrical waveform and stability of flagella in Chlamydomonas2014
Author(s)
Yanagisawa, H.A., Mathis, G., Oda, T., Hirono, M., Richey, E.A., Ishikawa, H., Marshall, W.F., Kikkawa, M., Qin, H.
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Journal Title
Mol. Biol. Cell
Volume: 25
Issue: 9
Pages: 1472-1483
DOI
Related Report
Peer Reviewed / Open Access / Acknowledgement Compliant
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[Journal Article] TTC26/DYF13 is an intraflagellar transport protein required for transport of motility-related proteins into flagella.2014
Author(s)
Ishikawa H, Ide T, Yagi T, Jiang X, Hirono M, Sasaki H, Yanagisawa H, Wemmer KA, Stainier DY, Qin H, Kamiya R, Marshall WF.
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Journal Title
Elife.
Volume: 3
Pages: 1-24
DOI
Related Report
Peer Reviewed / Open Access
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