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. Finally, key challenges and opportunities for METTL13 research are pinpointed in a prospective outlook.
Highlights
Cellular protein synthesis is guided and catalyzed by the ribosome, which uses messenger RNA as a template for protein synthesis in a process termed translation
The analysis revealed that cells lacking methyltransferase-like protein 13 (METTL13)-mediated eukaryotic elongation factor 1 alpha (eEF1A) methylation displayed a faster translation of histidine codons and a slower translation of alanine codons [11] (Figure 6)
Significant discoveries have been made to increase the understanding of METTL13 enzymatic activity, cellular features, and links to disease
Summary
Cellular protein synthesis is guided and catalyzed by the ribosome, which uses messenger RNA as a template for protein synthesis in a process termed translation. Methylation of lysine and the protein Nt are biochemically similar They both occur on primary amino groups corresponding to the α-amino group of the protein Nt and the ε-amino group of the lysine side chain (Figure 1C,D). Methylation of the Nt and lysine side chain have similar biochemical consequences. Trimethylation renders a permanent positive charge and chemically saturates the amino group making it chemically inert. Both sites can be acetylated by acetylCoA dependent acetyltransferases (Figure 1E). Nt and lysine acetylation renders the amino groups chemically inert by occupying the “free” election pair but, in contrast to methylation, acetylation neutralizes the positive charge (Figure 1F,G). We end with a prospective outlook and propose directions for future research
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