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Elongator and the role of its subcomplexes in human diseases

The Elongator complex was initially identified in yeast, and a variety of distinct cellular functions have been assigned to the complex. In the last decade, several research groups focussed on dissecting its structure, tRNA modification activity and role in translation regulation. Recently, Elongato...

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Autores principales: Gaik, Monika, Kojic, Marija, Wainwright, Brandon J, Glatt, Sebastian
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9906326/
https://www.ncbi.nlm.nih.gov/pubmed/36448458
http://dx.doi.org/10.15252/emmm.202216418
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author Gaik, Monika
Kojic, Marija
Wainwright, Brandon J
Glatt, Sebastian
author_facet Gaik, Monika
Kojic, Marija
Wainwright, Brandon J
Glatt, Sebastian
author_sort Gaik, Monika
collection PubMed
description The Elongator complex was initially identified in yeast, and a variety of distinct cellular functions have been assigned to the complex. In the last decade, several research groups focussed on dissecting its structure, tRNA modification activity and role in translation regulation. Recently, Elongator emerged as a crucial factor for various human diseases, and its involvement has triggered a strong interest in the complex from numerous clinical groups. The Elongator complex is highly conserved among eukaryotes, with all six subunits (Elp1‐6) contributing to its stability and function. Yet, recent studies have shown that the two subcomplexes, namely the catalytic Elp123 and accessory Elp456, may have distinct roles in the development of different neuronal subtypes. This Commentary aims to provide a brief overview and new perspectives for more systematic efforts to explore the functions of the Elongator in health and disease.
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spelling pubmed-99063262023-02-13 Elongator and the role of its subcomplexes in human diseases Gaik, Monika Kojic, Marija Wainwright, Brandon J Glatt, Sebastian EMBO Mol Med Commentary The Elongator complex was initially identified in yeast, and a variety of distinct cellular functions have been assigned to the complex. In the last decade, several research groups focussed on dissecting its structure, tRNA modification activity and role in translation regulation. Recently, Elongator emerged as a crucial factor for various human diseases, and its involvement has triggered a strong interest in the complex from numerous clinical groups. The Elongator complex is highly conserved among eukaryotes, with all six subunits (Elp1‐6) contributing to its stability and function. Yet, recent studies have shown that the two subcomplexes, namely the catalytic Elp123 and accessory Elp456, may have distinct roles in the development of different neuronal subtypes. This Commentary aims to provide a brief overview and new perspectives for more systematic efforts to explore the functions of the Elongator in health and disease. John Wiley and Sons Inc. 2022-11-30 /pmc/articles/PMC9906326/ /pubmed/36448458 http://dx.doi.org/10.15252/emmm.202216418 Text en © 2022 The Authors. Published under the terms of the CC BY 4.0 license. https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Commentary
Gaik, Monika
Kojic, Marija
Wainwright, Brandon J
Glatt, Sebastian
Elongator and the role of its subcomplexes in human diseases
title Elongator and the role of its subcomplexes in human diseases
title_full Elongator and the role of its subcomplexes in human diseases
title_fullStr Elongator and the role of its subcomplexes in human diseases
title_full_unstemmed Elongator and the role of its subcomplexes in human diseases
title_short Elongator and the role of its subcomplexes in human diseases
title_sort elongator and the role of its subcomplexes in human diseases
topic Commentary
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9906326/
https://www.ncbi.nlm.nih.gov/pubmed/36448458
http://dx.doi.org/10.15252/emmm.202216418
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