ArticleCell stress & chaperones2015
Convergent signaling pathways--interaction between methionine oxidation and serine/threonine/tyrosine O-phosphorylation.
Article in Cell stress & chaperones, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Protein turnover in plants-cost of synthesis, repair, and crop engineering opportunities.Plant physiology · 2026Review
- Reactive Oxygen Species (ROS) in Metabolic Disease-Don't Shoot the Metabolic Messenger.International journal of molecular sciences · 2025Review
- 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
- Profiling Dopamine-Induced Oxidized Proteoforms of β-synuclein by Top-Down Mass Spectrometry.Antioxidants (Basel, Switzerland) · 2021Article
- Shear Stress Ameliorates Superoxide Impairment to Erythrocyte Deformability With Concurrent Nitric Oxide Synthase Activation.Frontiers in physiology · 2019Article
- The phosphorylated redox proteome of Chlamydomonas reinhardtii: Revealing novel means for regulation of protein structure and function.Redox biology · 2018Article
- Methionine residues around phosphorylation sites are preferentially oxidized in vivo under stress conditions.Scientific reports · 2017Article
- Repression of the Chromatin-Tethering Domain of Murine Leukemia Virus p12.Journal of virology · 2016Article
- Sulphur Atoms from Methionines Interacting with Aromatic Residues Are Less Prone to Oxidation.Scientific reports · 2015Article
- Hepatic overexpression of methionine sulfoxide reductase A reduces atherosclerosis in apolipoprotein E-deficient mice.Journal of lipid research · 2015Article
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Authors and funding
4 authors.
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Abstract
Oxidation of methionine (Met) to Met sulfoxide (MetSO) is a frequently found reversible posttranslational modification. It has been presumed that the major functional role for oxidation-labile Met residues is to protect proteins/cells from oxidative stress. However, Met oxidation has been established as a key mechanism for direct regulation of a wide range of protein functions and cellular processes. Furthermore, recent reports suggest an interaction between Met oxidation and O-phosphorylation. Such interactions are a potentially direct interface between redox sensing and signaling, and cellular protein kinase/phosphatase-based signaling. Herein, we describe the current state of Met oxidation research, provide some mechanistic insight into crosstalk between these two major posttranslational modifications, and consider the evolutionary significance and regulatory potential of this crosstalk.
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