Polarity and asymmetry in the arrangement of dynein and related structures in the Chlamydomonas axoneme

Khanh Huy Bui; Toshiki Yagi; Ryosuke Yamamoto; Ritsu Kamiya; Takashi Ishikawa

@inproceedings{Bui2012PolarityAA, title={Polarity and asymmetry in the arrangement of dynein and related structures in the Chlamydomonas axoneme}, author={Khanh Huy Bui and Toshiki Yagi and Ryosuke Yamamoto and Ritsu Kamiya and Takashi Ishikawa}, booktitle={The Journal of cell biology}, year={2012} }

Understanding the molecular architecture of the flagellum is crucial to elucidate the bending mechanism produced by this complex organelle. The current known structure of the flagellum has not yet been fully correlated with the complex composition and localization of flagellar components. Using cryoelectron tomography and subtomogram averaging while distinguishing each one of the nine outer doublet microtubules, we systematically collected and reconstructed the three-dimensional structures in… CONTINUE READING

Mouse respiratory cilia with the asymmetric axonemal structure on sparsely distributed ciliary cells can generate overall directional flow.

Hironori Ueno, Takuji Ishikawa, Khanh Huy Bui, Kohsuke Gonda, Takashi Ishikawa, T. Yamaguchi
Nanomedicine : nanotechnology, biology, and…
2012

Polarity and asymmetry in the arrangement of dynein and related structures in the Chlamydomonas axoneme

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Systematic studies of all PIH proteins in zebrafish 1 reveal their distinct roles in axonemal dynein assembly 2 3 4

α- and β-Tubulin Lattice of the Axonemal Microtubule Doublet and Binding Proteins Revealed by Single Particle Cryo-Electron Microscopy and Tomography.

Functional diversity of axonemal dyneins as assessed by in vitro and in vivo motility assays of Chlamydomonas mutants.

The N-DRC forms a conserved biochemical complex that maintains outer doublet alignment and limits microtubule sliding in motile axonemes

General and specific promotion of flagellar assembly by a flagellar nucleoside diphosphate kinase

Cryo-electron tomography of motile cilia and flagella

Identification of the Outer-Inner Dynein Linker as a Hub Controller for Axonemal Dynein Activities

The MIA complex is a conserved and novel dynein regulator essential for normal ciliary motility

Tubulin polyglutamylation regulates flagellar motility by controlling a specific inner-arm dynein that interacts with the dynein regulatory complex.

A microtubule-dynein tethering complex regulates the axonemal inner dynein f (I1)

References

Publications referenced by this paper.

Comparative structural analysis of eukaryotic flagella and cilia from Chlamydomonas, Tetrahymena, and sea urchins.

Discrete PIH proteins function in the cytoplasmic preassembly of different subsets of axonemal dyneins

Asymmetry of inner dynein arms and inter-doublet links in Chlamydomonas flagella

Identification of dyneins that localize exclusively to the proximal portion of Chlamydomonas flagella.

Molecular architecture of inner dynein arms in situ in Chlamydomonas reinhardtii flagella

Mouse respiratory cilia with the asymmetric axonemal structure on sparsely distributed ciliary cells can generate overall directional flow.

SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields.

FLAGELLAR MOTION AND FINE STRUCTURE OF THE FLAGELLAR APPARATUS IN CHLAMYDOMONAS

Nucleotide-induced global conformational changes of flagellar dynein arms revealed by in situ analysis

The dynein regulatory complex is the nexin link and a major regulatory node in cilia and flagella