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

Axonemal dyneins must be precisely regulated and coordinated to produce ordered ciliary/flagellar motility, but how this is achieved is not understood. We analyzed two Chlamydomonas reinhardtii mutants, mia1 and mia2, which display slow swimming and low flagellar beat frequency. We found that the MI...

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Autores principales: Yamamoto, Ryosuke, Song, Kangkang, Yanagisawa, Haru-aki, Fox, Laura, Yagi, Toshiki, Wirschell, Maureen, Hirono, Masafumi, Kamiya, Ritsu, Nicastro, Daniela, Sale, Winfield S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3628515/
https://www.ncbi.nlm.nih.gov/pubmed/23569216
http://dx.doi.org/10.1083/jcb.201211048
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author Yamamoto, Ryosuke
Song, Kangkang
Yanagisawa, Haru-aki
Fox, Laura
Yagi, Toshiki
Wirschell, Maureen
Hirono, Masafumi
Kamiya, Ritsu
Nicastro, Daniela
Sale, Winfield S.
author_facet Yamamoto, Ryosuke
Song, Kangkang
Yanagisawa, Haru-aki
Fox, Laura
Yagi, Toshiki
Wirschell, Maureen
Hirono, Masafumi
Kamiya, Ritsu
Nicastro, Daniela
Sale, Winfield S.
author_sort Yamamoto, Ryosuke
collection PubMed
description Axonemal dyneins must be precisely regulated and coordinated to produce ordered ciliary/flagellar motility, but how this is achieved is not understood. We analyzed two Chlamydomonas reinhardtii mutants, mia1 and mia2, which display slow swimming and low flagellar beat frequency. We found that the MIA1 and MIA2 genes encode conserved coiled-coil proteins, FAP100 and FAP73, respectively, which form the modifier of inner arms (MIA) complex in flagella. Cryo–electron tomography of mia mutant axonemes revealed that the MIA complex was located immediately distal to the intermediate/light chain complex of I1 dynein and structurally appeared to connect with the nexin–dynein regulatory complex. In axonemes from mutants that lack both the outer dynein arms and the MIA complex, I1 dynein failed to assemble, suggesting physical interactions between these three axonemal complexes and a role for the MIA complex in the stable assembly of I1 dynein. The MIA complex appears to regulate I1 dynein and possibly outer arm dyneins, which are both essential for normal motility.
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spelling pubmed-36285152013-10-15 The MIA complex is a conserved and novel dynein regulator essential for normal ciliary motility Yamamoto, Ryosuke Song, Kangkang Yanagisawa, Haru-aki Fox, Laura Yagi, Toshiki Wirschell, Maureen Hirono, Masafumi Kamiya, Ritsu Nicastro, Daniela Sale, Winfield S. J Cell Biol Research Articles Axonemal dyneins must be precisely regulated and coordinated to produce ordered ciliary/flagellar motility, but how this is achieved is not understood. We analyzed two Chlamydomonas reinhardtii mutants, mia1 and mia2, which display slow swimming and low flagellar beat frequency. We found that the MIA1 and MIA2 genes encode conserved coiled-coil proteins, FAP100 and FAP73, respectively, which form the modifier of inner arms (MIA) complex in flagella. Cryo–electron tomography of mia mutant axonemes revealed that the MIA complex was located immediately distal to the intermediate/light chain complex of I1 dynein and structurally appeared to connect with the nexin–dynein regulatory complex. In axonemes from mutants that lack both the outer dynein arms and the MIA complex, I1 dynein failed to assemble, suggesting physical interactions between these three axonemal complexes and a role for the MIA complex in the stable assembly of I1 dynein. The MIA complex appears to regulate I1 dynein and possibly outer arm dyneins, which are both essential for normal motility. The Rockefeller University Press 2013-04-15 /pmc/articles/PMC3628515/ /pubmed/23569216 http://dx.doi.org/10.1083/jcb.201211048 Text en © 2013 Yamamoto et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).
spellingShingle Research Articles
Yamamoto, Ryosuke
Song, Kangkang
Yanagisawa, Haru-aki
Fox, Laura
Yagi, Toshiki
Wirschell, Maureen
Hirono, Masafumi
Kamiya, Ritsu
Nicastro, Daniela
Sale, Winfield S.
The MIA complex is a conserved and novel dynein regulator essential for normal ciliary motility
title The MIA complex is a conserved and novel dynein regulator essential for normal ciliary motility
title_full The MIA complex is a conserved and novel dynein regulator essential for normal ciliary motility
title_fullStr The MIA complex is a conserved and novel dynein regulator essential for normal ciliary motility
title_full_unstemmed The MIA complex is a conserved and novel dynein regulator essential for normal ciliary motility
title_short The MIA complex is a conserved and novel dynein regulator essential for normal ciliary motility
title_sort mia complex is a conserved and novel dynein regulator essential for normal ciliary motility
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3628515/
https://www.ncbi.nlm.nih.gov/pubmed/23569216
http://dx.doi.org/10.1083/jcb.201211048
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