ArticlePhilosophical transactions of the Royal Society of London. Series B, Biological sciences2012
Protein abundance is key to distinguish promiscuous from functional phosphorylation based on evolutionary information.
Article in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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47 citing papers in PubMed.
- The Constructive Neutral Evolution of Behaviour.Ecology and evolution · 2025Article
- The fitness cost of spurious phosphorylation.The EMBO journal · 2024Article
- Application of Machine Learning in the Quantitative Analysis of the Surface Characteristics of Highly Abundant Cytoplasmic Proteins: Toward AI-Based Biomimetics.Biomimetics (Basel, Switzerland) · 2024Article
- The fitness cost of spurious phosphorylation.bioRxiv : the preprint server for biology · 2023Article
- Key role of phosphorylation sites in ATPase domain and Linker region of MLH1 for DNA binding and functionality of MutLα.Scientific reports · 2023Article
- Evolutionary conservation of sequence motifs at sites of protein modification.The Journal of biological chemistry · 2023Article
- Fever as an evolutionary agent to select immune complexes interfaces.Immunogenetics · 2022Article
- Role of non-specific interactions in the phase-separation and maturation of macromolecules.PLoS computational biology · 2022Article
- Accurate, high-coverage assignment of in vivo protein kinases to phosphosites from in vitro phosphoproteomic specificity data.PLoS computational biology · 2022Article
- Are transient protein-protein interactions more dispensable?PLoS computational biology · 2022Article
- Evolutionary and functional lessons from human-specific amino acid substitution matrices.NAR genomics and bioinformatics · 2021Article
- Comparative transcriptome analysis and identification of candidate adaptive evolution genes ofPhysiology and molecular biology of plants : an international journal of functional plant biology · 2021Article
- Systematic Identification of Protein Phosphorylation-Mediated Interactions.Journal of proteome research · 2021Article
- In-depth and 3-dimensional exploration of the budding yeast phosphoproteome.EMBO reports · 2021Article
- Mutation Edgotype Drives Fitness Effect in Human.Frontiers in bioinformatics · 2021Article
- Article
- Phospho-Regulation of Meiotic Prophase.Frontiers in cell and developmental biology · 2021Review
- The evolutionary scaling of cellular traits imposed by the drift barrier.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- A Theoretical Framework for Evolutionary Cell Biology.Journal of molecular biology · 2020Review
- Multiple Site-Specific Phosphorylation of IDPs Monitored by NMR.Methods in molecular biology (Clifton, N.J.) · 2020Article
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3 authors.
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Abstract
In eukaryotic cells, protein phosphorylation is an important and widespread mechanism used to regulate protein function. Yet, of the thousands of phosphosites identified to date, only a few hundred at best have a characterized function. It was recently shown that these functional sites are significantly more conserved than phosphosites of unknown function, stressing the importance of considering evolutionary conservation in assessing the global functional landscape of phosphosites. This leads us to review studies that examined the impact of phosphorylation on evolutionary conservation. While all these studies have shown that conservation is greater among phosphorylated sites compared with non-phosphorylated ones, the magnitude of this difference varies greatly. Further, not all studies have considered key factors that may influence the rate of phosphosite evolution. Such key factors are their localization in ordered or disordered regions, their stoichiometry or the abundance of their corresponding protein. Here we take into account all of these factors simultaneously, which reveals remarkable evolutionary patterns. First, while it is well established that protein conservation increases with abundance, we show that phosphosites partly follow an opposite trend. More precisely, Saccharomyces cerevisiae phosphosites present among abundant proteins are 1.5 times more likely to diverge in the closely related species Saccharomyces bayanus when compared with phosphosites present in the 5 per cent least abundant proteins. Second, we show that conservation is coupled to stoichiometry, whereby sites frequently phosphorylated are more conserved than those rarely phosphorylated. Finally, we provide a model of functional and noisy or 'accidental' phosphorylation that explains these observations.
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