FAP206 is a microtubule-docking adapter for ciliary radial spoke 2 and dynein c
| Autor: | Ewa Joachimiak, Daniela Nicastro, Paulina Urbanska, Lea M. Alford, Winfield S. Sale, Jacek Gaertig, Todd M. Hennessey, Dorota Wloga, Kangkang Song, Erin E. Dymek, Krishna Kumar Vasudevan, Elizabeth F. Smith, William L. Dentler |
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| Rok vydání: | 2015 |
| Předmět: |
Models
Molecular Axoneme Electron Microscope Tomography Dynein Protozoan Proteins macromolecular substances Biology Microtubules Gene Knockout Techniques 03 medical and health sciences 0302 clinical medicine Adapter (genetics) Radial spoke Microtubule Cilia Molecular Biology Cytoskeleton 030304 developmental biology 0303 health sciences Cilium Dyneins Articles Cell Biology Cell biology Docking (molecular) Tetrahymena Dynactin 030217 neurology & neurosurgery |
| Zdroj: | Molecular Biology of the Cell |
| ISSN: | 1939-4586 1059-1524 |
| DOI: | 10.1091/mbc.e14-11-1506 |
| Popis: | Radial spokes are conserved macromolecular complexes that are essential for ciliary motility. Little is known about the assembly and functions of the three individual radial spokes, RS1, RS2, and RS3. In Tetrahymena, a conserved ciliary protein, FAP206, docks RS2 and dynein c to the doublet microtubule. Radial spokes are conserved macromolecular complexes that are essential for ciliary motility. A triplet of three radial spokes, RS1, RS2, and RS3, repeats every 96 nm along the doublet microtubules. Each spoke has a distinct base that docks to the doublet and is linked to different inner dynein arms. Little is known about the assembly and functions of individual radial spokes. A knockout of the conserved ciliary protein FAP206 in the ciliate Tetrahymena resulted in slow cell motility. Cryo–electron tomography showed that in the absence of FAP206, the 96-nm repeats lacked RS2 and dynein c. Occasionally, RS2 assembled but lacked both the front prong of its microtubule base and dynein c, whose tail is attached to the front prong. Overexpressed GFP-FAP206 decorated nonciliary microtubules in vivo. Thus FAP206 is likely part of the front prong and docks RS2 and dynein c to the microtubule. |
| Databáze: | OpenAIRE |
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