Structure, activity and function of the dual protein lysine and protein n‐terminal methyltransferase mettl13
(2021) In Life 11(11).- Abstract
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.... (More)
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.
(Less)
- author
- Jakobsson, Magnus E. LU
- organization
- publishing date
- 2021-11-01
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- EEF1A, Enzyme specificity, Lysine methylation, METTL13, N‐terminal methylation, Post translational modification, Translation
- in
- Life
- volume
- 11
- issue
- 11
- article number
- 1121
- publisher
- MDPI AG
- external identifiers
-
- pmid:34832997
- scopus:85118157781
- ISSN
- 0024-3019
- DOI
- 10.3390/life11111121
- language
- English
- LU publication?
- yes
- additional info
- Publisher Copyright: © 2021 by the author. Licensee MDPI, Basel, Switzerland.
- id
- da3c0189-8b32-4406-acb4-07bf65c98db4
- date added to LUP
- 2021-11-16 10:45:38
- date last changed
- 2024-06-29 21:27:22
@article{da3c0189-8b32-4406-acb4-07bf65c98db4,
abstract = {{<p>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.</p>}},
author = {{Jakobsson, Magnus E.}},
issn = {{0024-3019}},
keywords = {{EEF1A; Enzyme specificity; Lysine methylation; METTL13; N‐terminal methylation; Post translational modification; Translation}},
language = {{eng}},
month = {{11}},
number = {{11}},
publisher = {{MDPI AG}},
series = {{Life}},
title = {{Structure, activity and function of the dual protein lysine and protein n‐terminal methyltransferase mettl13}},
url = {{http://dx.doi.org/10.3390/life11111121}},
doi = {{10.3390/life11111121}},
volume = {{11}},
year = {{2021}},
}