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: Magnus E. Jakobsson
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Publicado: MDPI AG 2021
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Acceso en línea:https://doaj.org/article/fa746b5af7c747a58f040cfdbcd85a7e
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spelling oai:doaj.org-article:fa746b5af7c747a58f040cfdbcd85a7e2021-11-25T18:10:27ZStructure, Activity and Function of the Dual Protein Lysine and Protein N-Terminal Methyltransferase METTL1310.3390/life111111212075-1729https://doaj.org/article/fa746b5af7c747a58f040cfdbcd85a7e2021-10-01T00:00:00Zhttps://www.mdpi.com/2075-1729/11/11/1121https://doaj.org/toc/2075-1729METTL13 (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.Magnus E. JakobssonMDPI AGarticlepost translational modificationlysine methylationN-terminal methylationtranslationenzyme specificityeEF1AScienceQENLife, Vol 11, Iss 1121, p 1121 (2021)
institution DOAJ
collection DOAJ
language EN
topic post translational modification
lysine methylation
N-terminal methylation
translation
enzyme specificity
eEF1A
Science
Q
spellingShingle post translational modification
lysine methylation
N-terminal methylation
translation
enzyme specificity
eEF1A
Science
Q
Magnus E. Jakobsson
Structure, Activity and Function of the Dual Protein Lysine and Protein N-Terminal Methyltransferase METTL13
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.
format article
author Magnus E. Jakobsson
author_facet Magnus E. Jakobsson
author_sort Magnus E. Jakobsson
title 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_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_sort structure, activity and function of the dual protein lysine and protein n-terminal methyltransferase mettl13
publisher MDPI AG
publishDate 2021
url https://doaj.org/article/fa746b5af7c747a58f040cfdbcd85a7e
work_keys_str_mv AT magnusejakobsson structureactivityandfunctionofthedualproteinlysineandproteinnterminalmethyltransferasemettl13
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