ArticleDevelopmental cell2022
The evolutionarily conserved arginyltransferase 1 mediates a pVHL-independent oxygen-sensing pathway in mammalian cells.
Article in Developmental cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 14 citations in OpenAlex.
- The C-terminal domain of yeast Arginyltransferase1 is essential for its catalytic activity.FEBS open bio · 2026Article
- Trypsin exhibits exopeptidase-like activity toward N-terminal arginine that biases proteomic analyses.bioRxiv : the preprint server for biology · 2026Article
- Prolyl hydroxylase-dependent proteolysis enables the orthogonal hypoxia responses in plants.Nature communications · 2026Article
- Implementing N-terminomics and machine learning to probe Nt-arginylation.Nature communications · 2025Article
- Targeting endoplasmic reticulum stress and nitroso-redox imbalance in neuroendocrine prostate cancer: the therapeutic role of nitric oxide.Cell death discovery · 2025Article
- Arginyltransferase1 drives a mitochondria-dependent program to induce cell death.Cell death & disease · 2025Article
- The N-degron pathway mediates lipophagy: The chemical modulation of lipophagy in obesity and NAFLD.Metabolism: clinical and experimental · 2023Article
- Reconstitution of the Arginyltransferase (ATE1) Iron-Sulfur Cluster.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Assaying Arginylation Activity in Cell Lysates Using a Fluorescent Reporter.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Editorial: Waken the Silent Majority: Principles and Pathogenic Significance of Non-Acetyl Acylation and Other Understudied Post-Translational Modifications.Frontiers in cell and developmental biology · 2022Article
- The lower expression of circulating miR-210 and elevated serum levels of HIF-1α in ischemic stroke; Possible markers for diagnosis and disease prediction.Journal of clinical laboratory analysis · 2021Article
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Authors and funding
14 authors at 3 institutions in 1 country.
Funding
Abstract
The response to oxygen availability is a fundamental process concerning metabolism and survival/death in all mitochondria-containing eukaryotes. However, the known oxygen-sensing mechanism in mammalian cells depends on pVHL, which is only found among metazoans but not in other species. Here, we present an alternative oxygen-sensing pathway regulated by ATE1, an enzyme ubiquitously conserved in eukaryotes that influences protein degradation by posttranslational arginylation. We report that ATE1 centrally controls the hypoxic response and glycolysis in mammalian cells by preferentially arginylating HIF1α that is hydroxylated by PHD in the presence of oxygen. Furthermore, the degradation of arginylated HIF1α is independent of pVHL E3 ubiquitin ligase but dependent on the UBR family proteins. Bioinformatic analysis of human tumor data reveals that the ATE1/UBR and pVHL pathways jointly regulate oxygen sensing in a transcription-independent manner with different tissue specificities. Phylogenetic analysis suggests that eukaryotic ATE1 likely evolved during mitochondrial domestication, much earlier than pVHL.
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