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Structure, Activity and Function of the Dual Protein Lysine and Protein N-Terminal Methyltransferase METTL13

METTL13 (also known as eEF1A-KNMT and FEAT) is a dual methyltransferase reported to target the N-terminus and Lys55 in the eukaryotic translation elongation factor 1 alpha (eEF1A). METTL13-mediated methylation of eEF1A has functional consequences related to translation dynamics and include altered r...

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Autor principal: Jakobsson, Magnus E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8624817/
https://www.ncbi.nlm.nih.gov/pubmed/34832997
http://dx.doi.org/10.3390/life11111121
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author Jakobsson, Magnus E.
author_facet Jakobsson, Magnus E.
author_sort Jakobsson, Magnus E.
collection PubMed
description METTL13 (also known as eEF1A-KNMT and FEAT) is a dual methyltransferase reported to target the N-terminus and Lys55 in the eukaryotic translation elongation factor 1 alpha (eEF1A). METTL13-mediated methylation of eEF1A has functional consequences related to translation dynamics and include altered rate of global protein synthesis and translation of specific codons. Aberrant regulation of METTL13 has been linked to several types of cancer but the precise mechanisms are not yet fully understood. In this article, the current literature related to the structure, activity, and function of METTL13 is systematically reviewed and put into context. The links between METTL13 and diseases, mainly different types of cancer, are also summarized. Finally, key challenges and opportunities for METTL13 research are pinpointed in a prospective outlook.
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spelling pubmed-86248172021-11-27 Structure, Activity and Function of the Dual Protein Lysine and Protein N-Terminal Methyltransferase METTL13 Jakobsson, Magnus E. Life (Basel) Review METTL13 (also known as eEF1A-KNMT and FEAT) is a dual methyltransferase reported to target the N-terminus and Lys55 in the eukaryotic translation elongation factor 1 alpha (eEF1A). METTL13-mediated methylation of eEF1A has functional consequences related to translation dynamics and include altered rate of global protein synthesis and translation of specific codons. Aberrant regulation of METTL13 has been linked to several types of cancer but the precise mechanisms are not yet fully understood. In this article, the current literature related to the structure, activity, and function of METTL13 is systematically reviewed and put into context. The links between METTL13 and diseases, mainly different types of cancer, are also summarized. Finally, key challenges and opportunities for METTL13 research are pinpointed in a prospective outlook. MDPI 2021-10-21 /pmc/articles/PMC8624817/ /pubmed/34832997 http://dx.doi.org/10.3390/life11111121 Text en © 2021 by the author. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Jakobsson, Magnus E.
Structure, Activity and Function of the Dual Protein Lysine and Protein N-Terminal Methyltransferase METTL13
title Structure, Activity and Function of the Dual Protein Lysine and Protein N-Terminal Methyltransferase METTL13
title_full Structure, Activity and Function of the Dual Protein Lysine and Protein N-Terminal Methyltransferase METTL13
title_fullStr Structure, Activity and Function of the Dual Protein Lysine and Protein N-Terminal Methyltransferase METTL13
title_full_unstemmed Structure, Activity and Function of the Dual Protein Lysine and Protein N-Terminal Methyltransferase METTL13
title_short Structure, Activity and Function of the Dual Protein Lysine and Protein N-Terminal Methyltransferase METTL13
title_sort structure, activity and function of the dual protein lysine and protein n-terminal methyltransferase mettl13
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8624817/
https://www.ncbi.nlm.nih.gov/pubmed/34832997
http://dx.doi.org/10.3390/life11111121
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