期刊
MOLECULAR BIOLOGY OF THE CELL
卷 29, 期 9, 页码 1060-1074出版社
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E17-11-0689
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资金
- Kazato Research Foundation
- Takeda Science Foundation
- Japan Society for the Promotion of Science KAKENHI [15H01202, 17H05057, 17K15115]
- Naito Foundation
- Uehara Memorial Foundation
- Senri Life Science Foundation
- Institute for Fermentation, Osaka
- Ichiro Kanehara Foundation
- National Institutes of Health [R37 GM030626, R35 GM122574]
- Robert W. Booth Endowment at the University of Massachusetts Medical School
- Platform Project for Supporting Drug Discovery and Life Science Research (Basis for Supporting Innovative Drug Discovery and Life Science Research, BINDS) from the Japan Agency for Medical Research and Development, AMED
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R37GM030626, R35GM122574] Funding Source: NIH RePORTER
Motility of cilia/flagella is generated by a coordinated activity of thousands of dyneins. Inner dynein arms (IDAs) are particularly important for the formation of ciliary/flagellar waveforms, but the molecular mechanism of IDA regulation is poorly understood. Here we show using cryoelectron tomography and biochemical analyses of Chlamydomonas flagella that a conserved protein FAP44 forms a complex that tethers IDA f (I1 dynein) head domains to the A-tubule of the axonemal outer doublet microtubule. In wild-type flagella, IDA f showed little nucleotide-dependent movement except for a tilt in the f ss head perpendicular to the microtubule-sliding direction. In the absence of the tether complex, however, addition of ATP and vanadate caused a large conformational change in the IDA f head domains, suggesting that the movement of IDA f is mechanically restricted by the tether complex. Motility defects in flagella missing the tether demonstrates the importance of the IDA f-tether interaction in the regulation of ciliary/flagellar beating.
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