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FAP206 is a microtubule-docking adapter for ciliary radial spoke 2 and dynein c
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...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4325840/ https://www.ncbi.nlm.nih.gov/pubmed/25540426 http://dx.doi.org/10.1091/mbc.E14-11-1506 |
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author | Vasudevan, Krishna Kumar Song, Kangkang Alford, Lea M. Sale, Winfield S. Dymek, Erin E. Smith, Elizabeth F. Hennessey, Todd Joachimiak, Ewa Urbanska, Paulina Wloga, Dorota Dentler, William Nicastro, Daniela Gaertig, Jacek |
author_facet | Vasudevan, Krishna Kumar Song, Kangkang Alford, Lea M. Sale, Winfield S. Dymek, Erin E. Smith, Elizabeth F. Hennessey, Todd Joachimiak, Ewa Urbanska, Paulina Wloga, Dorota Dentler, William Nicastro, Daniela Gaertig, Jacek |
author_sort | Vasudevan, Krishna Kumar |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-4325840 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-43258402015-04-30 FAP206 is a microtubule-docking adapter for ciliary radial spoke 2 and dynein c Vasudevan, Krishna Kumar Song, Kangkang Alford, Lea M. Sale, Winfield S. Dymek, Erin E. Smith, Elizabeth F. Hennessey, Todd Joachimiak, Ewa Urbanska, Paulina Wloga, Dorota Dentler, William Nicastro, Daniela Gaertig, Jacek Mol Biol Cell Articles 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. The American Society for Cell Biology 2015-02-15 /pmc/articles/PMC4325840/ /pubmed/25540426 http://dx.doi.org/10.1091/mbc.E14-11-1506 Text en © 2015 Vasudevan, Song, et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. |
spellingShingle | Articles Vasudevan, Krishna Kumar Song, Kangkang Alford, Lea M. Sale, Winfield S. Dymek, Erin E. Smith, Elizabeth F. Hennessey, Todd Joachimiak, Ewa Urbanska, Paulina Wloga, Dorota Dentler, William Nicastro, Daniela Gaertig, Jacek FAP206 is a microtubule-docking adapter for ciliary radial spoke 2 and dynein c |
title | FAP206 is a microtubule-docking adapter for ciliary radial spoke 2 and dynein c |
title_full | FAP206 is a microtubule-docking adapter for ciliary radial spoke 2 and dynein c |
title_fullStr | FAP206 is a microtubule-docking adapter for ciliary radial spoke 2 and dynein c |
title_full_unstemmed | FAP206 is a microtubule-docking adapter for ciliary radial spoke 2 and dynein c |
title_short | FAP206 is a microtubule-docking adapter for ciliary radial spoke 2 and dynein c |
title_sort | fap206 is a microtubule-docking adapter for ciliary radial spoke 2 and dynein c |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4325840/ https://www.ncbi.nlm.nih.gov/pubmed/25540426 http://dx.doi.org/10.1091/mbc.E14-11-1506 |
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