ArticleBMC bioinformatics2013
Circles within circles: crosstalk between protein Ser/Thr/Tyr-phosphorylation and Met oxidation.
Article in BMC bioinformatics, 2013. 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.
- Are Methionine Sulfoxide-Containing Proteins Related to Seed Longevity? A Case Study ofPlants (Basel, Switzerland) · 2022Article
- Mitochondrial trafficking and redox/phosphorylation signaling supporting cell migration phenotypes.Frontiers in molecular biosciences · 2022Review
- Redox regulation of tyrosine kinase signalling: more than meets the eye.Journal of biochemistry · 2020Review
- Consequences of Oxidative Stress on Plant Glycolytic and Respiratory Metabolism.Frontiers in plant science · 2019Review
- Methionine residues around phosphorylation sites are preferentially oxidized in vivo under stress conditions.Scientific reports · 2017Article
- Sulphur Atoms from Methionines Interacting with Aromatic Residues Are Less Prone to Oxidation.Scientific reports · 2015Article
- Convergent signaling pathways--interaction between methionine oxidation and serine/threonine/tyrosine O-phosphorylation.Cell stress & chaperones · 2015Article
- Protein redox chemistry: post-translational cysteine modifications that regulate signal transduction and drug pharmacology.Frontiers in pharmacology · 2014Article
- In silico analysis of protein Lys-N(𝜀)-acetylation in plants.Frontiers in plant science · 2014Review
- Proceedings of the 2013 MidSouth Computational Biology and Bioinformatics Society (MCBIOS) Conference.BMC bioinformatics · 2013Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundReversible posttranslational protein modifications such as phosphorylation of Ser/Thr/Tyr and Met oxidation are critical for both metabolic regulation and cellular signalling. Although these modifications are typically studied individually, herein we describe the potential for cross-talk and hierarchical regulation.
resultsThe proximity of Met to Ser/Thr/Tyr within the proteome has not previously been addressed. In order to consider the possibility of a generalized interaction, we performed a trans-kingdom sequence analysis of known phosphorylation sites in proteins from bacteria, fungi, plants, and animals. The proportion of phosphorylation sites that include a Met within a 13-residue window centered upon Ser/Thr/Tyr is significantly less than the occurrence of Met in proximity to all Ser/Thr/Tyr residues. Met residues are present at all positions (-6 to +6, inclusive) within the 13-residue window that we have considered. Detailed analysis of sequences from eight disparate plant taxa revealed that many conserved phosphorylation sites have a Met residue in the proximity. Results from GO enrichment analysis indicated that the potential for phosphorylation and Met oxidation crosstalk is most prevalent in kinases and proteins involved in signalling.
conclusionThe large proportion of known phosphorylation sites with Met in the proximity fulfils the necessary condition for cross-talk. Kinases/signalling proteins are enriched for Met around phosphorylation sites. These proteins/sites are likely candidates for cross-talk between oxidative signalling and reversible phosphorylation.
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