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Structure and function of outer dynein arm intermediate and light chain complex

The outer dynein arm (ODA) is a molecular complex that drives the beating motion of cilia/flagella. Chlamydomonas ODA is composed of three heavy chains (HCs), two ICs, and 11 light chains (LCs). Although the three-dimensional (3D) structure of the whole ODA complex has been investigated, the 3D conf...

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Autores principales: Oda, Toshiyuki, Abe, Tatsuki, Yanagisawa, Haruaki, Kikkawa, Masahide
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4814214/
https://www.ncbi.nlm.nih.gov/pubmed/26864626
http://dx.doi.org/10.1091/mbc.E15-10-0723
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author Oda, Toshiyuki
Abe, Tatsuki
Yanagisawa, Haruaki
Kikkawa, Masahide
author_facet Oda, Toshiyuki
Abe, Tatsuki
Yanagisawa, Haruaki
Kikkawa, Masahide
author_sort Oda, Toshiyuki
collection PubMed
description The outer dynein arm (ODA) is a molecular complex that drives the beating motion of cilia/flagella. Chlamydomonas ODA is composed of three heavy chains (HCs), two ICs, and 11 light chains (LCs). Although the three-dimensional (3D) structure of the whole ODA complex has been investigated, the 3D configurations of the ICs and LCs are largely unknown. Here we identified the 3D positions of the two ICs and three LCs using cryo–electron tomography and structural labeling. We found that these ICs and LCs were all localized at the root of the outer-inner dynein (OID) linker, designated the ODA-Beak complex. Of interest, the coiled-coil domain of IC2 extended from the ODA-Beak to the outer surface of ODA. Furthermore, we investigated the molecular mechanisms of how the OID linker transmits signals to the ODA-Beak, by manipulating the interaction within the OID linker using a chemically induced dimerization system. We showed that the cross-linking of the OID linker strongly suppresses flagellar motility in vivo. These results suggest that the ICs and LCs of the ODA form the ODA-Beak, which may be involved in mechanosignaling from the OID linker to the HCs.
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spelling pubmed-48142142016-06-16 Structure and function of outer dynein arm intermediate and light chain complex Oda, Toshiyuki Abe, Tatsuki Yanagisawa, Haruaki Kikkawa, Masahide Mol Biol Cell Brief Report The outer dynein arm (ODA) is a molecular complex that drives the beating motion of cilia/flagella. Chlamydomonas ODA is composed of three heavy chains (HCs), two ICs, and 11 light chains (LCs). Although the three-dimensional (3D) structure of the whole ODA complex has been investigated, the 3D configurations of the ICs and LCs are largely unknown. Here we identified the 3D positions of the two ICs and three LCs using cryo–electron tomography and structural labeling. We found that these ICs and LCs were all localized at the root of the outer-inner dynein (OID) linker, designated the ODA-Beak complex. Of interest, the coiled-coil domain of IC2 extended from the ODA-Beak to the outer surface of ODA. Furthermore, we investigated the molecular mechanisms of how the OID linker transmits signals to the ODA-Beak, by manipulating the interaction within the OID linker using a chemically induced dimerization system. We showed that the cross-linking of the OID linker strongly suppresses flagellar motility in vivo. These results suggest that the ICs and LCs of the ODA form the ODA-Beak, which may be involved in mechanosignaling from the OID linker to the HCs. The American Society for Cell Biology 2016-04-01 /pmc/articles/PMC4814214/ /pubmed/26864626 http://dx.doi.org/10.1091/mbc.E15-10-0723 Text en © 2016 Oda 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 Brief Report
Oda, Toshiyuki
Abe, Tatsuki
Yanagisawa, Haruaki
Kikkawa, Masahide
Structure and function of outer dynein arm intermediate and light chain complex
title Structure and function of outer dynein arm intermediate and light chain complex
title_full Structure and function of outer dynein arm intermediate and light chain complex
title_fullStr Structure and function of outer dynein arm intermediate and light chain complex
title_full_unstemmed Structure and function of outer dynein arm intermediate and light chain complex
title_short Structure and function of outer dynein arm intermediate and light chain complex
title_sort structure and function of outer dynein arm intermediate and light chain complex
topic Brief Report
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4814214/
https://www.ncbi.nlm.nih.gov/pubmed/26864626
http://dx.doi.org/10.1091/mbc.E15-10-0723
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