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The hydrolethalus syndrome protein HYLS-1 regulates formation of the ciliary gate
Transition fibres (TFs), together with the transition zone (TZ), are basal ciliary structures thought to be crucial for cilium biogenesis and function by acting as a ciliary gate to regulate selective protein entry and exit. Here we demonstrate that the centriolar and basal body protein HYLS-1, the...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4992140/ https://www.ncbi.nlm.nih.gov/pubmed/27534274 http://dx.doi.org/10.1038/ncomms12437 |
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author | Wei, Qing Zhang, Yingyi Schouteden, Clementine Zhang, Yuxia Zhang, Qing Dong, Jinhong Wonesch, Veronika Ling, Kun Dammermann, Alexander Hu, Jinghua |
author_facet | Wei, Qing Zhang, Yingyi Schouteden, Clementine Zhang, Yuxia Zhang, Qing Dong, Jinhong Wonesch, Veronika Ling, Kun Dammermann, Alexander Hu, Jinghua |
author_sort | Wei, Qing |
collection | PubMed |
description | Transition fibres (TFs), together with the transition zone (TZ), are basal ciliary structures thought to be crucial for cilium biogenesis and function by acting as a ciliary gate to regulate selective protein entry and exit. Here we demonstrate that the centriolar and basal body protein HYLS-1, the C. elegans orthologue of hydrolethalus syndrome protein 1, is required for TF formation, TZ organization and ciliary gating. Loss of HYLS-1 compromises the docking and entry of intraflagellar transport (IFT) particles, ciliary gating for both membrane and soluble proteins, and axoneme assembly. Additional depletion of the TF component DYF-19 in hyls-1 mutants further exacerbates TZ anomalies and completely abrogates ciliogenesis. Our data support an important role for HYLS-1 and TFs in establishment of the ciliary gate and underline the importance of selective protein entry for cilia assembly. |
format | Online Article Text |
id | pubmed-4992140 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-49921402016-09-01 The hydrolethalus syndrome protein HYLS-1 regulates formation of the ciliary gate Wei, Qing Zhang, Yingyi Schouteden, Clementine Zhang, Yuxia Zhang, Qing Dong, Jinhong Wonesch, Veronika Ling, Kun Dammermann, Alexander Hu, Jinghua Nat Commun Article Transition fibres (TFs), together with the transition zone (TZ), are basal ciliary structures thought to be crucial for cilium biogenesis and function by acting as a ciliary gate to regulate selective protein entry and exit. Here we demonstrate that the centriolar and basal body protein HYLS-1, the C. elegans orthologue of hydrolethalus syndrome protein 1, is required for TF formation, TZ organization and ciliary gating. Loss of HYLS-1 compromises the docking and entry of intraflagellar transport (IFT) particles, ciliary gating for both membrane and soluble proteins, and axoneme assembly. Additional depletion of the TF component DYF-19 in hyls-1 mutants further exacerbates TZ anomalies and completely abrogates ciliogenesis. Our data support an important role for HYLS-1 and TFs in establishment of the ciliary gate and underline the importance of selective protein entry for cilia assembly. Nature Publishing Group 2016-08-18 /pmc/articles/PMC4992140/ /pubmed/27534274 http://dx.doi.org/10.1038/ncomms12437 Text en Copyright © 2016, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Wei, Qing Zhang, Yingyi Schouteden, Clementine Zhang, Yuxia Zhang, Qing Dong, Jinhong Wonesch, Veronika Ling, Kun Dammermann, Alexander Hu, Jinghua The hydrolethalus syndrome protein HYLS-1 regulates formation of the ciliary gate |
title | The hydrolethalus syndrome protein HYLS-1 regulates formation of the ciliary gate |
title_full | The hydrolethalus syndrome protein HYLS-1 regulates formation of the ciliary gate |
title_fullStr | The hydrolethalus syndrome protein HYLS-1 regulates formation of the ciliary gate |
title_full_unstemmed | The hydrolethalus syndrome protein HYLS-1 regulates formation of the ciliary gate |
title_short | The hydrolethalus syndrome protein HYLS-1 regulates formation of the ciliary gate |
title_sort | hydrolethalus syndrome protein hyls-1 regulates formation of the ciliary gate |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4992140/ https://www.ncbi.nlm.nih.gov/pubmed/27534274 http://dx.doi.org/10.1038/ncomms12437 |
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