{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\n Eukaryotic elongation factor 1α (eEF1A) is known to be extensively modified by lysine methylation, a post‐translational modification that regulates its role in translation and may impact additional cellular processes. One of the key enzymes in this multilayered modification system is EEF1A‐KMT1, formerly annotated as N6AMT2. This enzyme specifically catalyzes the trimethylation of lysine 79 on eEF1A, a modification that is conserved from yeast to human and is indicative of an evolutionarily maintained function."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": " Although the precise regulatory consequences of Lys79 trimethylation remain to be fully defined, its conservation suggests that EEF1A‐KMT1 plays an important role in fine‐tuning the translational machinery. Notably, the methylation landscape of eEF1A is complex, with other enzymes such as METTL21B, which targets Lys165, and eEF1A‐KMT4, which modifies Lys36, further underscoring the significance of lysine methylation in modulating eEF1A functions."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}]}, {"type": "t", "text": " Together, these studies support a model in which multiple, site‐specific methylation events—mediated by distinct methyltransferases such as EEF1A‐KMT1—cooperatively regulate both the canonical role of eEF1A in protein synthesis and its non‐canonical functions, thereby providing an additional layer of control over cellular homeostasis.\n "}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Joshua J Hamey, Daniel L Winter, Daniel Yagoub, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Novel N-terminal and Lysine Methyltransferases That Target Translation Elongation Factor 1A in Yeast and Human."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Proteomics (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/mcp.M115.052449"}], "href": "https://doi.org/10.1074/mcp.M115.052449"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26545399"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26545399"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Jedrzej Malecki, Vinay Kumar Aileni, Angela Y Y Ho, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The novel lysine specific methyltransferase METTL21B affects mRNA translation through inducible and dynamic methylation of Lys-165 in human eukaryotic elongation factor 1 alpha (eEF1A)."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nucleic Acids Res (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/nar/gkx002"}], "href": "https://doi.org/10.1093/nar/gkx002"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28108655"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28108655"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Magnus E Jakobsson, Jedrzej Malecki, Benedikt S Nilges, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Methylation of human eukaryotic elongation factor alpha (eEF1A) by a member of a novel protein lysine methyltransferase family modulates mRNA translation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nucleic Acids Res (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/nar/gkx432"}], "href": "https://doi.org/10.1093/nar/gkx432"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28520920"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28520920"}]}]}]}