ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2012
Modular evolution of phosphorylation-based signalling systems.
Review 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 82 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
82 citing papers in PubMed, 164 citations in OpenAlex.
- Alternative splicing fine-tunes modular protein interfaces to control protein localization.Nature structural & molecular biology · 2026Article
- Phosphoproteome-derived peptide libraries for deep specificity profiling of phosphatases and phospholyases.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Mechanistic design of cell-penetrating disruptors for phospho-dependent TACC3-CHC interaction.Structure (London, England : 1993) · 2026Article
- Central Dogma Cycle and Network: A Model for Cell Memory.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- Differential phosphorylation of PHIP phosphopeptides with implications in insulin signaling.BMC molecular and cell biology · 2026Article
- Article
- Exploration of phosphoproteomic association during epimorphic regeneration.Scientific reports · 2025Article
- Conservation of OFD1 Protein Motifs: Implications for Discovery of Novel Interactors and the OFD1 Function.International journal of molecular sciences · 2025Article
- Multi-Omics Analysis Reveals Immune Infiltration and Clinical Significance of Phosphorylation Modification Enzymes in Lung Adenocarcinoma.International journal of molecular sciences · 2025Article
- Molecular docking and dynamics in protein serine/threonine kinase drug discovery: advances, challenges, and future perspectives.Frontiers in pharmacology · 2025Review
- Functional Role of Protein Phosphatase-6 (Current medicinal chemistry · 2025Review
- Substrate recognition principles for the PP2A-B55 protein phosphatase.Science advances · 2024Article
- Protein posttranslational modifications in metabolic diseases: basic concepts and targeted therapies.MedComm · 2024Review
- An improved bacterial mRNA enrichment strategy in dual RNA sequencing to unveil the dynamics of plant-bacterial interactions.Plant methods · 2024Article
- Structured Tandem Repeats in Protein Interactions.International journal of molecular sciences · 2024Article
- Mining oomycete proteomes for phosphatome leads to the identification of specific expanded phosphatases in oomycetes.Molecular plant pathology · 2024Article
- The PP2A-like phosphatase Ppg1 mediates assembly of the Far complex to balance gluconeogenic outputs and enables adaptation to glucose depletion.PLoS genetics · 2024Article
- The druggability of SH2 domains unmasked.Nature chemical biology · 2024Article
- Article
- The function of alternative splicing in the proteome: rewiring protein interactomes to put old functions into new contexts.Nature structural & molecular biology · 2023Review
22 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Phosphorylation sites are formed by protein kinases ('writers'), frequently exert their effects following recognition by phospho-binding proteins ('readers') and are removed by protein phosphatases ('erasers'). This writer-reader-eraser toolkit allows phosphorylation events to control a broad range of regulatory processes, and has been pivotal in the evolution of new functions required for the development of multi-cellular animals. The proteins that comprise this system of protein kinases, phospho-binding targets and phosphatases are typically modular in organization, in the sense that they are composed of multiple globular domains and smaller peptide motifs with binding or catalytic properties. The linkage of these binding and catalytic modules in new ways through genetic recombination, and the selection of particular domain combinations, has promoted the evolution of novel, biologically useful processes. Conversely, the joining of domains in aberrant combinations can subvert cell signalling and be causative in diseases such as cancer. Major inventions such as phosphotyrosine (pTyr)-mediated signalling that flourished in the first multi-cellular animals and their immediate predecessors resulted from stepwise evolutionary progression. This involved changes in the binding properties of interaction domains such as SH2 and their linkage to new domain types, and alterations in the catalytic specificities of kinases and phosphatases. This review will focus on the modular aspects of signalling networks and the mechanism by which they may have evolved.
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Registered trials
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.