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Axonemal radial spokes: 3D structure, function and assembly

The radial spoke (RS) is a complex of at least 23 proteins that works as a mechanochemical transducer between the central‐pair apparatus and the peripheral microtubule doublets in eukaryotic flagella and motile cilia. The RS contributes to the regulation of the activity of dynein motors, and thus to...

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Detalles Bibliográficos
Autores principales: Pigino, Gaia, Ishikawa, Takashi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Landes Bioscience 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3383722/
https://www.ncbi.nlm.nih.gov/pubmed/22754630
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author Pigino, Gaia
Ishikawa, Takashi
author_facet Pigino, Gaia
Ishikawa, Takashi
author_sort Pigino, Gaia
collection PubMed
description The radial spoke (RS) is a complex of at least 23 proteins that works as a mechanochemical transducer between the central‐pair apparatus and the peripheral microtubule doublets in eukaryotic flagella and motile cilia. The RS contributes to the regulation of the activity of dynein motors, and thus to flagellar motility. Despite numerous biochemical, physiological and structural studies, the mechanism of the function of the radial spoke remains unclear. Detailed knowledge of the 3D structure of the RS protein complex is needed in order to understand how RS regulates dynein activity. Here we review the most important findings on the structure of the RS, including results of our recent cryo‐electron tomographic analysis of the RS protein complex.
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spelling pubmed-33837222012-06-29 Axonemal radial spokes: 3D structure, function and assembly Pigino, Gaia Ishikawa, Takashi Bioarchitecture Review The radial spoke (RS) is a complex of at least 23 proteins that works as a mechanochemical transducer between the central‐pair apparatus and the peripheral microtubule doublets in eukaryotic flagella and motile cilia. The RS contributes to the regulation of the activity of dynein motors, and thus to flagellar motility. Despite numerous biochemical, physiological and structural studies, the mechanism of the function of the radial spoke remains unclear. Detailed knowledge of the 3D structure of the RS protein complex is needed in order to understand how RS regulates dynein activity. Here we review the most important findings on the structure of the RS, including results of our recent cryo‐electron tomographic analysis of the RS protein complex. Landes Bioscience 2012-02-01 /pmc/articles/PMC3383722/ /pubmed/22754630 Text en Copyright © 2012 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.
spellingShingle Review
Pigino, Gaia
Ishikawa, Takashi
Axonemal radial spokes: 3D structure, function and assembly
title Axonemal radial spokes: 3D structure, function and assembly
title_full Axonemal radial spokes: 3D structure, function and assembly
title_fullStr Axonemal radial spokes: 3D structure, function and assembly
title_full_unstemmed Axonemal radial spokes: 3D structure, function and assembly
title_short Axonemal radial spokes: 3D structure, function and assembly
title_sort axonemal radial spokes: 3d structure, function and assembly
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3383722/
https://www.ncbi.nlm.nih.gov/pubmed/22754630
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