ArticleScientific reports2017
Methionine residues around phosphorylation sites are preferentially oxidized in vivo under stress conditions.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 71 citations in OpenAlex.
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- Role of Redox-Induced Protein Modifications in Spermatozoa in Health and Disease.Antioxidants (Basel, Switzerland) · 2025Review
- Methionine Antagonizes Liver and Kidney Antioxidant Function Damage in Heat-Stressed Rex Rabbits.Animals : an open access journal from MDPI · 2025Article
- Murine hepatic proteome adaptation to high-fat diets with different contents of saturated fatty acids and linoleic acid : α-linolenic acid polyunsaturated fatty acid ratios.Journal of veterinary research · 2024Article
- The association of protein-bound methionine sulfoxide with proteomic basis for aging in beech seeds.BMC plant biology · 2024Article
- Methionine Sulfoxide Reductases Suppress the Formation of the [Antioxidants (Basel, Switzerland) · 2023Article
- Metamorphism in TDP-43 prion-like domain determines chaperone recognition.Nature communications · 2023Article
- An Activity-Based Oxaziridine Platform for Identifying and Developing Covalent Ligands for Functional Allosteric Methionine Sites: Redox-Dependent Inhibition of Cyclin-Dependent Kinase 4.Journal of the American Chemical Society · 2022Article
- Accurate Proteomewide Measurement of Methionine Oxidation in Aging Mouse Brains.Journal of proteome research · 2022Article
- Phylogenies from unaligned proteomes using sequence environments of amino acid residues.Scientific reports · 2022Article
- Protein folding stabilities are a major determinant of oxidation rates for buried methionine residues.The Journal of biological chemistry · 2022Article
- Are Methionine Sulfoxide-Containing Proteins Related to Seed Longevity? A Case Study ofPlants (Basel, Switzerland) · 2022Article
- Mitochondrial ROS control neuronal excitability and cell fate in frontotemporal dementia.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2022Article
- Characterization of adenine phosphoribosyltransferase (APRT) activity in Trypanosoma brucei brucei: Only one of the two isoforms is kinetically active.PLoS neglected tropical diseases · 2022Article
- The Role of Methionine Residues in the Regulation of Liquid-Liquid Phase Separation.Biomolecules · 2021Review
- Profiling Dopamine-Induced Oxidized Proteoforms of β-synuclein by Top-Down Mass Spectrometry.Antioxidants (Basel, Switzerland) · 2021Article
- Effect of Met/Leu substitutions on the stability of NAD+-dependent formate dehydrogenases from Gossypium hirsutum.Applied microbiology and biotechnology · 2021Article
- Systematic Identification of Protein Phosphorylation-Mediated Interactions.Journal of proteome research · 2021Article
- Involvement of the MetO/Msr System in TwoInternational journal of molecular sciences · 2020Article
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Authors and funding
3 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Protein phosphorylation is one of the most prevalent and well-understood protein modifications. Oxidation of protein-bound methionine, which has been traditionally perceived as an inevitable damage derived from oxidative stress, is now emerging as another modification capable of regulating protein activity during stress conditions. However, the mechanism coupling oxidative signals to changes in protein function remains unknown. An appealing hypothesis is that methionine oxidation might serve as a rheostat to control phosphorylation. To investigate this potential crosstalk between phosphorylation and methionine oxidation, we have addressed the co-occurrence of these two types of modifications within the human proteome. Here, we show that nearly all (98%) proteins containing oxidized methionine were also phosphoproteins. Furthermore, phosphorylation sites were much closer to oxidized methionines when compared to non-oxidized methionines. This proximity between modification sites cannot be accounted for by their co-localization within unstructured clusters because it was faithfully reproduced in a smaller sample of structured proteins. We also provide evidence that the oxidation of methionine located within phosphorylation motifs is a highly selective process among stress-related proteins, which supports the hypothesis of crosstalk between methionine oxidation and phosphorylation as part of the cellular defence against oxidative stress.
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