ArticleMolecular and cellular biology1996
Conformational changes induced in the protein tyrosine kinase p72syk by tyrosine phosphorylation or by binding of phosphorylated immunoreceptor tyrosine-based activation motif peptides.
Article in Molecular and cellular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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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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Who cites it
35 citing papers in PubMed, 120 citations in OpenAlex.
- Activation of AKT via a dual mechanism enhances the susceptibility of melanoma cells to glucose deprivation.Cell death & disease · 2025Article
- hFcγRIIa: a double-edged sword in osteoclastogenesis and bone balance in transgenic mice.Frontiers in immunology · 2024Article
- Docking of Syk to FcεRI is enhanced by Lyn but limited in duration by SHIP1.Molecular biology of the cell · 2022Article
- Identification of Inhibitors of Integrin Cytoplasmic Domain Interactions With Syk.Frontiers in immunology · 2020Article
- IgE and IgG Antibodies as Regulators of Mast Cell and Basophil Functions in Food Allergy.Frontiers in immunology · 2020Review
- Receptors That Inhibit Macrophage Activation: Mechanisms and Signals of Regulation and Tolerance.Journal of immunology research · 2018Review
- The FcεRI Signaling Cascade and Integrin Trafficking Converge at Patterned Ligand Surfaces.Molecular biology of the cell · 2017Article
- Phosphorylation impact on Spleen Tyrosine kinase conformation by Surface Enhanced Raman Spectroscopy.Scientific reports · 2017Article
- Of ITIMs, ITAMs, and ITAMis: revisiting immunoglobulin Fc receptor signaling.Immunological reviews · 2015Review
- Shifting FcγRIIA-ITAM from activation to inhibitory configuration ameliorates arthritis.The Journal of clinical investigation · 2014Article
- Once phosphorylated, tyrosines in carboxyl terminus of protein-tyrosine kinase Syk interact with signaling proteins, including TULA-2, a negative regulator of mast cell degranulation.The Journal of biological chemistry · 2012Article
- Regulation and function of syk tyrosine kinase in mast cell signaling and beyond.Journal of signal transduction · 2011Article
- Mast cell signaling: the role of protein tyrosine kinase Syk, its activation and screening methods for new pathway participants.FEBS letters · 2010Review
- Tyrosines in the carboxyl terminus regulate Syk kinase activity and function.The Journal of biological chemistry · 2010Article
- TREM2- and DAP12-dependent activation of PI3K requires DAP10 and is inhibited by SHIP1.Science signaling · 2010Article
- FcepsilonRI-induced activation by low antigen concentrations results in nuclear signals in the absence of degranulation.Molecular immunology · 2009Article
- Real-time cross-correlation image analysis of early events in IgE receptor signaling.Biophysical journal · 2008Article
- The kinase Syk as an adaptor controlling sustained calcium signalling and B-cell development.The EMBO journal · 2008Article
- 3D structure of Syk kinase determined by single-particle electron microscopy.Biochimica et biophysica acta · 2007Article
- Binding of a diphosphorylated-ITAM peptide to spleen tyrosine kinase (Syk) induces distal conformational changes: a hydrogen exchange mass spectrometry study.Journal of the American Society for Mass Spectrometry · 2005Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A critical event in signaling in immune cells is the interaction of Syk or ZAP-70 protein tyrosine kinases with multisubunit receptors that contain an approximately 18-amino-acid domain called the immunoreceptor tyrosine-based activation motif (ITAM). Tyrosine-phosphorylated Syk from activated cells was in a conformation different from that in nonstimulated cells as demonstrated by changes in immunoreactivity. The addition of tyrosine-diphosphorylated ITAM peptides resulted in a similar conformational change in Syk from nonactivated cells. The peptides based on FcepsilonRIgamma were more active than those based on Fcepsilon RIbeta. In vitro autophosphorylation of Syk was dramatically enhanced by the addition of the diphosphorylated ITAM peptides. The conformational change and the enhanced autophosphorylation required the presence of both phosphorylated tyrosines on the same molecule. These conformational changes in Syk by tyrosine phosphorylation or binding to diphosphorylated ITAM could be critical for Syk activation and downstream propagation of intracellular signals.
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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.