ArticleNucleic acids research2017
Methylation of human eukaryotic elongation factor alpha (eEF1A) by a member of a novel protein lysine methyltransferase family modulates mRNA translation.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 56 citations in OpenAlex.
- EEF1AKMT4-eEF1A2 synergistically facilitates the progression of GBC by promoting ribosomal protein output.Genes & diseases · 2026Article
- Update of the Methyltransferase Gene Family: Classification, Evolution and Biological Functions.Human genomics · 2026Review
- A transcriptomic and proteomic map of primary human cell types.Nucleic acids research · 2026Article
- Epigenetic, ribosomal, and immune dysregulation in paediatric acute-onset neuropsychiatric syndrome.Molecular psychiatry · 2025Article
- Experience-mediated transcriptional memory correlates with hypoxia resistance in the nervous system of the sea hareAmerican journal of physiology. Regulatory, integrative and comparative physiology · 2025Article
- Differential susceptibility to prenatal stress exposure in serotonin transporter-deficient female mice-an epigenetic exploration.Frontiers in neuroscience · 2025Article
- Closing in on human methylation-the versatile family of seven-β-strand (METTL) methyltransferases.Nucleic acids research · 2024Review
- METTL Family in Healthy and Disease.Molecular biomedicine · 2024Review
- The protein methylation network in yeast: A landmark in completeness for a eukaryotic post-translational modification.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- METTL13 facilitates cell growth and metastasis in gastric cancer via an eEF1A/HN1L positive feedback circuit.Journal of cell communication and signaling · 2023Article
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- Protein methylation in mitochondria.The Journal of biological chemistry · 2022Review
- SETD2 regulates the methylation of translation elongation factor eEF1A1 in clear cell renal cell carcinoma.Kidney cancer journal : official journal of the Kidney Cancer Association · 2022Article
- Multiomics analysis reveals the mechanical stress-dependent changes in trabecular meshwork cytoskeletal-extracellular matrix interactions.Frontiers in cell and developmental biology · 2022Article
- Proteomic profiling and correlations with clinical features reveal biomarkers indicative of diabetic retinopathy with diabetic kidney disease.Frontiers in endocrinology · 2022Article
- Structure, Activity and Function of the Dual Protein Lysine and Protein N-Terminal Methyltransferase METTL13.Life (Basel, Switzerland) · 2021Review
- Large-scale identification of protein histidine methylation in human cells.NAR genomics and bioinformatics · 2021Article
- Evidence for a synergistic effect of post-translational modifications and genomic composition of eEF-1α on the adaptation ofEcology and evolution · 2021Article
- Human METTL18 is a histidine-specific methyltransferase that targets RPL3 and affects ribosome biogenesis and function.Nucleic acids research · 2021Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many cellular proteins are methylated on lysine residues and this has been most intensively studied for histone proteins. Lysine methylations on non-histone proteins are also frequent, but in most cases the functional significance of the methylation event, as well as the identity of the responsible lysine (K) specific methyltransferase (KMT), remain unknown. Several recently discovered KMTs belong to the so-called seven-β-strand (7BS) class of MTases and we have here investigated an uncharacterized human 7BS MTase currently annotated as part of the endothelin converting enzyme 2, but which should be considered a separate enzyme. Combining in vitro enzymology and analyzes of knockout cells, we demonstrate that this MTase efficiently methylates K36 in eukaryotic translation elongation factor 1 alpha (eEF1A) in vitro and in vivo. We suggest that this novel KMT is named eEF1A-KMT4 (gene name EEF1AKMT4), in agreement with the recently established nomenclature. Furthermore, by ribosome profiling we show that the absence of K36 methylation affects translation dynamics and changes translation speed of distinct codons. Finally, we show that eEF1A-KMT4 is part of a novel family of human KMTs, defined by a shared sequence motif in the active site and we demonstrate the importance of this motif for catalytic activity.
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