ArticleProceedings of the National Academy of Sciences of the United States of America2014
Sudestada1, a Drosophila ribosomal prolyl-hydroxylase required for mRNA translation, cell homeostasis, and organ growth.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. 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, 52 citations in OpenAlex.
- OGFOD1: a critical mediator of chemoresistance in acute myeloid leukemia.Frontiers in pharmacology · 2026Article
- Recent Advances and Therapeutic Implications of 2-Oxoglutarate-Dependent Dioxygenases in Ischemic Stroke.Molecular neurobiology · 2024Review
- Inhibition of OGFOD1 by FG4592 confers neuroprotection by activating unfolded protein response and autophagy after ischemic stroke.Journal of translational medicine · 2024Article
- Oxidation Products of Tryptophan and Proline in Adipokinetic Hormones-Artifacts or Post-Translational Modifications?Life (Basel, Switzerland) · 2023Article
- OGFOD1 modulates the transcriptional and proteomic landscapes to alter isoproterenol-induced hypertrophy susceptibility.Journal of molecular and cellular cardiology · 2023Article
- Fear-of-intimacy-mediated zinc transport is required for Drosophila fat body endoreplication.BMC biology · 2023Article
- Ogfod1 deletion increases cardiac beta-alanine levels and protects mice against ischaemia- reperfusion injury.Cardiovascular research · 2022Article
- Article
- Iron in Translation: From the Beginning to the End.Microorganisms · 2021Review
- Oxygen sensing in crustaceans: functions and mechanisms.Journal of comparative physiology. A, Neuroethology, sensory, neural, and behavioral physiology · 2021Review
- Human 2-oxoglutarate-dependent oxygenases: nutrient sensors, stress responders, and disease mediators.Biochemical Society transactions · 2020Review
- A human protein hydroxylase that accepts D-residues.Communications chemistry · 2020Article
- Review
- Mechanisms of hypoxia signalling: new implications for nephrology.Nature reviews. Nephrology · 2019Review
- Selective Inhibitors of a Human Prolyl Hydroxylase (OGFOD1) Involved in Ribosomal Decoding.Chemistry (Weinheim an der Bergstrasse, Germany) · 2019Article
- Amazing Diversity in Biochemical Roles of Fe(II)/2-Oxoglutarate Oxygenases.Trends in biochemical sciences · 2018Review
- The Jumonji-C oxygenase JMJD7 catalyzes (3S)-lysyl hydroxylation of TRAFAC GTPases.Nature chemical biology · 2018Article
- Phylogenetic and genomic analyses of the ribosomal oxygenases Riox1 (No66) and Riox2 (Mina53) provide new insights into their evolution.BMC evolutionary biology · 2018Article
- YcfDExtremophiles : life under extreme conditions · 2018Article
- Article
Corrections and comments
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Authors and funding
17 authors at 3 institutions in 2 countries.
Funding
Abstract
Genome sequences predict the presence of many 2-oxoglutarate (2OG)-dependent oxygenases of unknown biochemical and biological functions in Drosophila. Ribosomal protein hydroxylation is emerging as an important 2OG oxygenase catalyzed pathway, but its biological functions are unclear. We report investigations on the function of Sudestada1 (Sud1), a Drosophila ribosomal oxygenase. As with its human and yeast homologs, OGFOD1 and Tpa1p, respectively, we identified Sud1 to catalyze prolyl-hydroxylation of the small ribosomal subunit protein RPS23. Like OGFOD1, Sud1 catalyzes a single prolyl-hydroxylation of RPS23 in contrast to yeast Tpa1p, where Pro-64 dihydroxylation is observed. RNAi-mediated Sud1 knockdown hinders normal growth in different Drosophila tissues. Growth impairment originates from both reduction of cell size and diminution of the number of cells and correlates with impaired translation efficiency and activation of the unfolded protein response in the endoplasmic reticulum. This is accompanied by phosphorylation of eIF2α and concomitant formation of stress granules, as well as promotion of autophagy and apoptosis. These observations, together with those on enzyme homologs described in the companion articles, reveal conserved biochemical and biological roles for a widely distributed ribosomal oxygenase.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.