ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2012
Evolution of SH2 domains and phosphotyrosine signalling networks.
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 48 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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
48 citing papers in PubMed, 85 citations in OpenAlex.
- PI(3,5)PScience advances · 2026Article
- Discovery of a sulfotyrosine-motif in the human TrkB extracellular domain required for agonist activation.bioRxiv : the preprint server for biology · 2026Article
- Update on Structure and Function of SH2 Domains: Mechanisms and Emerging Targeting Strategies.International journal of molecular sciences · 2025Review
- Deletion of SH2D5 alleviates epileptic seizures and NMDAR expression via autophagic degradation of STAT1.JCI insight · 2025Article
- Article
- Development and Applications of Chimera Platforms for Tyrosine Phosphorylation.ACS central science · 2023Article
- The role of forkhead-associated (FHA)-domain proteins in plant biology.Plant molecular biology · 2023Review
- Article
- The Molten Globule State of a Globular Protein in a Cell Is More or Less Frequent Case Rather than an Exception.Molecules (Basel, Switzerland) · 2022Review
- The relative binding position of Nck and Grb2 adaptors impacts actin-based motility of Vaccinia virus.eLife · 2022Article
- Domain Analysis and Motif Matcher (DAMM): A Program to Predict Selectivity Determinants inMolecules (Basel, Switzerland) · 2021Article
- Importance of tyrosine phosphorylation for transmembrane signaling in plants.The Biochemical journal · 2021Review
- The claudin-transcription factor signaling pathway.Tissue barriers · 2021Review
- DomainViz: intuitive visualization of consensus domain distributions across groups of proteins.Nucleic acids research · 2021Article
- The GTPase-activating protein p120RasGAP has an evolutionarily conserved "FLVR-unique" SH2 domain.The Journal of biological chemistry · 2020Article
- SH2 Domain Binding: Diverse FLVRs of Partnership.Frontiers in endocrinology · 2020Review
- Exploring protein phosphorylation by combining computational approaches and biochemical methods.Computational and structural biotechnology journal · 2020Article
- The multiple functions of the numerousMicrobial cell (Graz, Austria) · 2019Review
- Tyrosine Phosphorylation of CD2AP Affects Stability of the Slit Diaphragm Complex.Journal of the American Society of Nephrology : JASN · 2019Article
- Review
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
Src homology 2 (SH2) domains mediate selective protein-protein interactions with tyrosine phosphorylated proteins, and in doing so define specificity of phosphotyrosine (pTyr) signalling networks. SH2 domains and protein-tyrosine phosphatases expand alongside protein-tyrosine kinases (PTKs) to coordinate cellular and organismal complexity in the evolution of the unikont branch of the eukaryotes. Examination of conserved families of PTKs and SH2 domain proteins provides fiduciary marks that trace the evolutionary landscape for the development of complex cellular systems in the proto-metazoan and metazoan lineages. The evolutionary provenance of conserved SH2 and PTK families reveals the mechanisms by which diversity is achieved through adaptations in tissue-specific gene transcription, altered ligand binding, insertions of linear motifs and the gain or loss of domains following gene duplication. We discuss mechanisms by which pTyr-mediated signalling networks evolve through the development of novel and expanded families of SH2 domain proteins and the elaboration of connections between pTyr-signalling proteins. These changes underlie the variety of general and specific signalling networks that give rise to tissue-specific functions and increasingly complex developmental programmes. Examination of SH2 domains from an evolutionary perspective provides insight into the process by which evolutionary expansion and modification of molecular protein interaction domain proteins permits the development of novel protein-interaction networks and accommodates adaptation of signalling networks.
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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.