The inner junction complex of the cilia is an interaction hub that involves tubulin post-translational modifications

Microtubules are cytoskeletal structures involved in stability, transport and organization in the cell. The building blocks, the α- and β-tubulin heterodimers, form protofilaments that associate laterally into the hollow microtubule. Microtubule also exists as highly stable doublet microtubules in t...

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Published in:	eLife Vol. 9
Main Authors:	Khalifa, Ahmad Abdelzaher Zaki, Ichikawa, Muneyoshi, Dai, Daniel, Kubo, Shintaroh, Black, Corbin Steven, Peri, Katya, McAlear, Thomas S, Veyron, Simon, Yang, Shun Kai, Vargas, Javier, Bechstedt, Susanne, Trempe, Jean-François, Bui, Khanh Huy
Format:	Journal Article
Language:	English
Published:	England eLife Sciences Publications Ltd 17-01-2020 eLife Sciences Publications, Ltd
Subjects:	acetylation axoneme Bioinformatics Chlamydomonas reinhardtii - metabolism Cilia Cilia - metabolism Computational Biology Cryoelectron Microscopy - methods Cytoskeleton Defects doublet microtubule Electron microscopy inner junction Localization Mass Spectrometry Mass spectroscopy Microtubules Microtubules - metabolism Motility Plant Proteins - metabolism Post-translation Protein Processing, Post-Translational Proteins Protozoan Proteins - metabolism Structural Biology and Molecular Biophysics Tetrahymena thermophila Tetrahymena thermophila - metabolism Translation Tubules Tubulin acetylation Tetrahymena thermophila inner junction axoneme cilia doublet microtubule structural biology chlamydomonas reinhardtii molecular biophysics
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Abstract	Microtubules are cytoskeletal structures involved in stability, transport and organization in the cell. The building blocks, the α- and β-tubulin heterodimers, form protofilaments that associate laterally into the hollow microtubule. Microtubule also exists as highly stable doublet microtubules in the cilia where stability is needed for ciliary beating and function. The doublet microtubule maintains its stability through interactions at its inner and outer junctions where its A- and B-tubules meet. Here, using cryo-electron microscopy, bioinformatics and mass spectrometry of the doublets of and , we identified two new inner junction proteins, FAP276 and FAP106, and an inner junction-associated protein, FAP126, thus presenting the complete answer to the inner junction identity and localization. Our structural study of the doublets shows that the inner junction serves as an interaction hub that involves tubulin post-translational modifications. These interactions contribute to the stability of the doublet and hence, normal ciliary motility.
AbstractList	Microtubules are cytoskeletal structures involved in stability, transport and organization in the cell. The building blocks, the α- and β-tubulin heterodimers, form protofilaments that associate laterally into the hollow microtubule. Microtubule also exists as highly stable doublet microtubules in the cilia where stability is needed for ciliary beating and function. The doublet microtubule maintains its stability through interactions at its inner and outer junctions where its A- and B-tubules meet. Here, using cryo-electron microscopy, bioinformatics and mass spectrometry of the doublets of Chlamydomonas reinhardtii and Tetrahymena thermophila, we identified two new inner junction proteins, FAP276 and FAP106, and an inner junction-associated protein, FAP126, thus presenting the complete answer to the inner junction identity and localization. Our structural study of the doublets shows that the inner junction serves as an interaction hub that involves tubulin post-translational modifications. These interactions contribute to the stability of the doublet and hence, normal ciliary motility. Microtubules are cytoskeletal structures involved in stability, transport and organization in the cell. The building blocks, the α- and β-tubulin heterodimers, form protofilaments that associate laterally into the hollow microtubule. Microtubule also exists as highly stable doublet microtubules in the cilia where stability is needed for ciliary beating and function. The doublet microtubule maintains its stability through interactions at its inner and outer junctions where its A- and B-tubules meet. Here, using cryo-electron microscopy, bioinformatics and mass spectrometry of the doublets of Chlamydomonas reinhardtii and Tetrahymena thermophila , we identified two new inner junction proteins, FAP276 and FAP106, and an inner junction-associated protein, FAP126, thus presenting the complete answer to the inner junction identity and localization. Our structural study of the doublets shows that the inner junction serves as an interaction hub that involves tubulin post-translational modifications. These interactions contribute to the stability of the doublet and hence, normal ciliary motility. Microtubules are cytoskeletal structures involved in stability, transport and organization in the cell. The building blocks, the α- and β-tubulin heterodimers, form protofilaments that associate laterally into the hollow microtubule. Microtubule also exists as highly stable doublet microtubules in the cilia where stability is needed for ciliary beating and function. The doublet microtubule maintains its stability through interactions at its inner and outer junctions where its A- and B-tubules meet. Here, using cryo-electron microscopy, bioinformatics and mass spectrometry of the doublets of and , we identified two new inner junction proteins, FAP276 and FAP106, and an inner junction-associated protein, FAP126, thus presenting the complete answer to the inner junction identity and localization. Our structural study of the doublets shows that the inner junction serves as an interaction hub that involves tubulin post-translational modifications. These interactions contribute to the stability of the doublet and hence, normal ciliary motility.
Author	Bechstedt, Susanne Yang, Shun Kai Peri, Katya Black, Corbin Steven Dai, Daniel Bui, Khanh Huy Khalifa, Ahmad Abdelzaher Zaki McAlear, Thomas S Trempe, Jean-François Vargas, Javier Kubo, Shintaroh Ichikawa, Muneyoshi Veyron, Simon
Author_xml	– sequence: 1 givenname: Ahmad Abdelzaher Zaki orcidid: 0000-0001-5569-2014 surname: Khalifa fullname: Khalifa, Ahmad Abdelzaher Zaki organization: Centre de Recherche en Biologie Structurale - FRQS, McGill University, Québec, Canada – sequence: 2 givenname: Muneyoshi orcidid: 0000-0002-5921-7699 surname: Ichikawa fullname: Ichikawa, Muneyoshi organization: Department of Anatomy and Cell Biology, McGill University, Québec, Canada – sequence: 3 givenname: Daniel orcidid: 0000-0002-9973-0446 surname: Dai fullname: Dai, Daniel organization: Centre de Recherche en Biologie Structurale - FRQS, McGill University, Québec, Canada – sequence: 4 givenname: Shintaroh orcidid: 0000-0002-0946-8879 surname: Kubo fullname: Kubo, Shintaroh organization: Department of Biophysics, Graduate School of Science, Kyoto University, Kyoto, Japan – sequence: 5 givenname: Corbin Steven orcidid: 0000-0003-2777-6434 surname: Black fullname: Black, Corbin Steven organization: Centre de Recherche en Biologie Structurale - FRQS, McGill University, Québec, Canada – sequence: 6 givenname: Katya orcidid: 0000-0002-7367-7501 surname: Peri fullname: Peri, Katya organization: Department of Anatomy and Cell Biology, McGill University, Québec, Canada – sequence: 7 givenname: Thomas S orcidid: 0000-0001-6097-0103 surname: McAlear fullname: McAlear, Thomas S organization: Centre de Recherche en Biologie Structurale - FRQS, McGill University, Québec, Canada – sequence: 8 givenname: Simon orcidid: 0000-0002-5533-5268 surname: Veyron fullname: Veyron, Simon organization: Department of Pharmacology & Therapeutics, McGill University, Montréal, Canada – sequence: 9 givenname: Shun Kai orcidid: 0000-0002-2363-1441 surname: Yang fullname: Yang, Shun Kai organization: Centre de Recherche en Biologie Structurale - FRQS, McGill University, Québec, Canada – sequence: 10 givenname: Javier orcidid: 0000-0001-7519-6106 surname: Vargas fullname: Vargas, Javier organization: Centre de Recherche en Biologie Structurale - FRQS, McGill University, Québec, Canada – sequence: 11 givenname: Susanne orcidid: 0000-0002-4706-9975 surname: Bechstedt fullname: Bechstedt, Susanne organization: Centre de Recherche en Biologie Structurale - FRQS, McGill University, Québec, Canada – sequence: 12 givenname: Jean-François orcidid: 0000-0002-6543-3371 surname: Trempe fullname: Trempe, Jean-François organization: Department of Pharmacology & Therapeutics, McGill University, Montréal, Canada – sequence: 13 givenname: Khanh Huy orcidid: 0000-0003-2814-9889 surname: Bui fullname: Bui, Khanh Huy organization: Centre de Recherche en Biologie Structurale - FRQS, McGill University, Québec, Canada
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/31951202$$D View this record in MEDLINE/PubMed
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Copyright	2020, Khalifa et al. 2020, Khalifa et al. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. 2020, Khalifa et al 2020 Khalifa et al
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Keywords	acetylation Tetrahymena thermophila inner junction axoneme cilia doublet microtubule structural biology chlamydomonas reinhardtii molecular biophysics
Language	English
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Notes	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 These authors contributed equally to this work. Department of Systems Biology, Graduate School of Biological Sciences, Nara Institute of Science and Technology, Nara, Japan.
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Snippet	Microtubules are cytoskeletal structures involved in stability, transport and organization in the cell. The building blocks, the α- and β-tubulin heterodimers,...
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SubjectTerms	acetylation axoneme Bioinformatics Chlamydomonas reinhardtii - metabolism Cilia Cilia - metabolism Computational Biology Cryoelectron Microscopy - methods Cytoskeleton Defects doublet microtubule Electron microscopy inner junction Localization Mass Spectrometry Mass spectroscopy Microtubules Microtubules - metabolism Motility Plant Proteins - metabolism Post-translation Protein Processing, Post-Translational Proteins Protozoan Proteins - metabolism Structural Biology and Molecular Biophysics Tetrahymena thermophila Tetrahymena thermophila - metabolism Translation Tubules Tubulin
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Title	The inner junction complex of the cilia is an interaction hub that involves tubulin post-translational modifications
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