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-Structure paper
Title | A microtubule-dynein tethering complex regulates the axonemal inner dynein f (I1). |
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Journal, issue, pages | Mol Biol Cell, Vol. 29, Issue 9, Page 1060-1074, Year 2018 |
Publish date | May 1, 2018 |
![]() | Tomohiro Kubo / Yuqing Hou / Deborah A Cochran / George B Witman / Toshiyuki Oda / ![]() ![]() |
PubMed Abstract | 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 ...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 β 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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Methods | EM (subtomogram averaging) |
Resolution | 40.0 - 60.0 Å |
Structure data | ![]() EMDB-6866: ![]() EMDB-6867: ![]() EMDB-6868: ![]() EMDB-6869: ![]() EMDB-6870: ![]() EMDB-6871: ![]() EMDB-6872: ![]() EMDB-6873: ![]() EMDB-6874: |
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