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Tubulin glycylation controls primary cilia length
As essential components of the eukaryotic cytoskeleton, microtubules fulfill a variety of functions that can be temporally and spatially controlled by tubulin posttranslational modifications. Tubulin glycylation has so far been mostly found on motile cilia and flagella, where it is involved in the s...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5584158/ https://www.ncbi.nlm.nih.gov/pubmed/28687664 http://dx.doi.org/10.1083/jcb.201612050 |
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author | Gadadhar, Sudarshan Dadi, Hala Bodakuntla, Satish Schnitzler, Anne Bièche, Ivan Rusconi, Filippo Janke, Carsten |
author_facet | Gadadhar, Sudarshan Dadi, Hala Bodakuntla, Satish Schnitzler, Anne Bièche, Ivan Rusconi, Filippo Janke, Carsten |
author_sort | Gadadhar, Sudarshan |
collection | PubMed |
description | As essential components of the eukaryotic cytoskeleton, microtubules fulfill a variety of functions that can be temporally and spatially controlled by tubulin posttranslational modifications. Tubulin glycylation has so far been mostly found on motile cilia and flagella, where it is involved in the stabilization of the axoneme. In contrast, barely anything is known about the role of glycylation in primary cilia because of limitations in detecting this modification in these organelles. We thus developed novel glycylation-specific antibodies with which we detected glycylation in many primary cilia. Glycylation accumulates in primary cilia in a length-dependent manner, and depletion or overexpression of glycylating enzymes modulates the length of primary cilia in cultured cells. This strongly suggests that glycylation is essential for the homeostasis of primary cilia, which has important implications for human disorders related to primary cilia dysfunctions, such as ciliopathies and certain types of cancer. |
format | Online Article Text |
id | pubmed-5584158 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-55841582018-03-04 Tubulin glycylation controls primary cilia length Gadadhar, Sudarshan Dadi, Hala Bodakuntla, Satish Schnitzler, Anne Bièche, Ivan Rusconi, Filippo Janke, Carsten J Cell Biol Research Articles As essential components of the eukaryotic cytoskeleton, microtubules fulfill a variety of functions that can be temporally and spatially controlled by tubulin posttranslational modifications. Tubulin glycylation has so far been mostly found on motile cilia and flagella, where it is involved in the stabilization of the axoneme. In contrast, barely anything is known about the role of glycylation in primary cilia because of limitations in detecting this modification in these organelles. We thus developed novel glycylation-specific antibodies with which we detected glycylation in many primary cilia. Glycylation accumulates in primary cilia in a length-dependent manner, and depletion or overexpression of glycylating enzymes modulates the length of primary cilia in cultured cells. This strongly suggests that glycylation is essential for the homeostasis of primary cilia, which has important implications for human disorders related to primary cilia dysfunctions, such as ciliopathies and certain types of cancer. The Rockefeller University Press 2017-09-04 /pmc/articles/PMC5584158/ /pubmed/28687664 http://dx.doi.org/10.1083/jcb.201612050 Text en © 2017 Gadadhar et al. http://www.rupress.org/terms/https://creativecommons.org/licenses/by-nc-sa/4.0/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 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Research Articles Gadadhar, Sudarshan Dadi, Hala Bodakuntla, Satish Schnitzler, Anne Bièche, Ivan Rusconi, Filippo Janke, Carsten Tubulin glycylation controls primary cilia length |
title | Tubulin glycylation controls primary cilia length |
title_full | Tubulin glycylation controls primary cilia length |
title_fullStr | Tubulin glycylation controls primary cilia length |
title_full_unstemmed | Tubulin glycylation controls primary cilia length |
title_short | Tubulin glycylation controls primary cilia length |
title_sort | tubulin glycylation controls primary cilia length |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5584158/ https://www.ncbi.nlm.nih.gov/pubmed/28687664 http://dx.doi.org/10.1083/jcb.201612050 |
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