ArticleThe Journal of biological chemistry2022
EGLN1 prolyl hydroxylation of hypoxia-induced transcription factor HIF1α is repressed by SET7-catalyzed lysine methylation.
Article in The Journal of biological chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Epigenetic dichotomy in florid vs. gliotic proliferative diabetic retinopathy: hypomethylation of EGLN1 and MMP9 drives divergent pathogenic pathways in angiogenesis and fibrosis.Frontiers in endocrinology · 2026Article
- Prediction of all-cause in-hospital mortality after ICU admission and 1-year mortality after discharge of patients with acute kidney injury.Renal failure · 2025Article
- Validation and the role of PDK4 relevant to ferroptosis in degenerative lumbar disc disease.Journal of orthopaedic surgery and research · 2025Article
- Salidroside rescues hypoxic cardiomyocytes by regulating the EGLN1/HIF‑1α pathway.Biomedical reports · 2024Article
- Analyzing the molecular mechanism of Scutellaria Radix in the treatment of sepsis using RNA sequencing.BMC infectious diseases · 2024Article
- Critical insights on "Association of the C allele of rs479200 in the EGLN1 gene with COVID‑19 severity in Indian population: a novel finding".Human genomics · 2024Article
- Single-Cell Analyses Offer Insights into the Different Remodeling Programs of Arteries and Veins.Cells · 2024Article
- Prolyl hydroxylase domain enzyme PHD2 inhibits proliferation and metabolism in non-small cell lung cancer cells in HIF-dependent and HIF-independent manners.Frontiers in oncology · 2024Article
- Comparative Analysis of Water Extracts from Roselle (International journal of molecular sciences · 2023Article
Corrections and comments
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Authors and funding
12 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Egg-laying defective nine 1 (EGLN1) functions as an oxygen sensor to catalyze prolyl hydroxylation of the transcription factor hypoxia-inducible factor-1 α under normoxia conditions, leading to its proteasomal degradation. Thus, EGLN1 plays a central role in the hypoxia-inducible factor-mediated hypoxia signaling pathway; however, the posttranslational modifications that control EGLN1 function remain largely unknown. Here, we identified that a lysine monomethylase, SET7, catalyzes EGLN1 methylation on lysine 297, resulting in the repression of EGLN1 activity in catalyzing prolyl hydroxylation of hypoxia-inducible factor-1 α. Notably, we demonstrate that the methylation mimic mutant of EGLN1 loses the capability to suppress the hypoxia signaling pathway, leading to the enhancement of cell proliferation and the oxygen consumption rate. Collectively, our data identify a novel modification of EGLN1 that is critical for inhibiting its enzymatic activity and which may benefit cellular adaptation to conditions of hypoxia.
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