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Regulation of tubulin glutamylation plays cell-specific roles in the function and stability of sensory cilia
Microtubules (MTs) are post-translationally modified, but the functions of post-translational modifications (PTMs) have in many cases remained unknown. Most PTMs, such as polyglutamylation, occur on the protruding C-terminal tail (CTT) of tubulins, are reversible, and have been proposed to play a ro...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Landes Bioscience
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3670407/ https://www.ncbi.nlm.nih.gov/pubmed/24058841 http://dx.doi.org/10.4161/worm.19539 |
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author | O’Hagan, Robert Barr, Maureen M. |
author_facet | O’Hagan, Robert Barr, Maureen M. |
author_sort | O’Hagan, Robert |
collection | PubMed |
description | Microtubules (MTs) are post-translationally modified, but the functions of post-translational modifications (PTMs) have in many cases remained unknown. Most PTMs, such as polyglutamylation, occur on the protruding C-terminal tail (CTT) of tubulins, are reversible, and have been proposed to play a role in regulation of MT-associated proteins (MAPs), molecular motors, and MT-severing proteins. Several PTM enzymes have been identified, including a carboxypeptidase in mice known as CCP1, which reduces polyglutamylation on the CTT of MTs, and causes cell-specific neurodegeneration when mutated. |
format | Online Article Text |
id | pubmed-3670407 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Landes Bioscience |
record_format | MEDLINE/PubMed |
spelling | pubmed-36704072013-09-19 Regulation of tubulin glutamylation plays cell-specific roles in the function and stability of sensory cilia O’Hagan, Robert Barr, Maureen M. Worm Commentary Microtubules (MTs) are post-translationally modified, but the functions of post-translational modifications (PTMs) have in many cases remained unknown. Most PTMs, such as polyglutamylation, occur on the protruding C-terminal tail (CTT) of tubulins, are reversible, and have been proposed to play a role in regulation of MT-associated proteins (MAPs), molecular motors, and MT-severing proteins. Several PTM enzymes have been identified, including a carboxypeptidase in mice known as CCP1, which reduces polyglutamylation on the CTT of MTs, and causes cell-specific neurodegeneration when mutated. Landes Bioscience 2012-07-01 /pmc/articles/PMC3670407/ /pubmed/24058841 http://dx.doi.org/10.4161/worm.19539 Text en Copyright © 2012 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited. |
spellingShingle | Commentary O’Hagan, Robert Barr, Maureen M. Regulation of tubulin glutamylation plays cell-specific roles in the function and stability of sensory cilia |
title | Regulation of tubulin glutamylation plays cell-specific roles in the function and stability of sensory cilia |
title_full | Regulation of tubulin glutamylation plays cell-specific roles in the function and stability of sensory cilia |
title_fullStr | Regulation of tubulin glutamylation plays cell-specific roles in the function and stability of sensory cilia |
title_full_unstemmed | Regulation of tubulin glutamylation plays cell-specific roles in the function and stability of sensory cilia |
title_short | Regulation of tubulin glutamylation plays cell-specific roles in the function and stability of sensory cilia |
title_sort | regulation of tubulin glutamylation plays cell-specific roles in the function and stability of sensory cilia |
topic | Commentary |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3670407/ https://www.ncbi.nlm.nih.gov/pubmed/24058841 http://dx.doi.org/10.4161/worm.19539 |
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