ArticleProceedings of the National Academy of Sciences of the United States of America1994
Aggregation of the high-affinity IgE receptor and enhanced activity of p53/56lyn protein-tyrosine kinase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 177 citations in OpenAlex.
- Suppression of IgE-mediated anaphylaxis and food allergy with monovalent anti-FcεRIα mAbs.The Journal of allergy and clinical immunology · 2021Article
- The Two Isoforms of Lyn Display Different Intramolecular Fuzzy Complexes with the SH3 Domain.Molecules (Basel, Switzerland) · 2018Article
- IgG-Independent Co-aggregation of FcεRI and FcγRIIB Results in LYN- and SHIP1-Dependent Tyrosine Phosphorylation of FcγRIIB in Murine Bone Marrow-Derived Mast Cells.Frontiers in immunology · 2018Article
- Differential mast cell outcomes are sensitive to FcεRI-Syk binding kinetics.Molecular biology of the cell · 2017Article
- Functional nanoscale coupling of Lyn kinase with IgE-FcεRI is restricted by the actin cytoskeleton in early antigen-stimulated signaling.Molecular biology of the cell · 2016Article
- Differential Lyn-dependence of the SHIP1-deficient mast cell phenotype.Cell communication and signaling : CCS · 2016Article
- Transmembrane adaptor protein PAG/CBP is involved in both positive and negative regulation of mast cell signaling.Molecular and cellular biology · 2014Article
- Activation/Inhibition of mast cells by supra-optimal antigen concentrations.Cell communication and signaling : CCS · 2013Article
- Quantitative nanoscale analysis of IgE-FcεRI clustering and coupling to early signaling proteins.The journal of physical chemistry. B · 2012Article
- Article
- Mast cell chemotaxis - chemoattractants and signaling pathways.Frontiers in immunology · 2012Article
- Transmembrane adaptor proteins in the high-affinity IgE receptor signaling.Frontiers in immunology · 2011Article
- A detailed mathematical model predicts that serial engagement of IgE-Fc epsilon RI complexes can enhance Syk activation in mast cells.Journal of immunology (Baltimore, Md. : 1950) · 2010Article
- Functional analysis of Lyn kinase A and B isoforms reveals redundant and distinct roles in Fc epsilon RI-dependent mast cell activation.Journal of immunology (Baltimore, Md. : 1950) · 2010Article
- The SCHOOL of nature: I. Transmembrane signaling.Self/nonself · 2010Article
- Adapters in the organization of mast cell signaling.Immunological reviews · 2009Review
- Differential dephosphorylation of the FcRgamma immunoreceptor tyrosine-based activation motif tyrosines with dissimilar potential for activating Syk.The Journal of biological chemistry · 2008Article
- A mechanism for SRC kinase-dependent signaling by noncatalytic receptors.Biochemistry · 2008Review
- G protein-coupled receptors and the modification of FcepsilonRI-mediated mast cell activation.Immunology letters · 2007Review
- Quantitative time-resolved phosphoproteomic analysis of mast cell signaling.Journal of immunology (Baltimore, Md. : 1950) · 2007Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aggregation of the receptor with high affinity for IgE (Fc epsilon RI) on the surface of mast cells and basophils stimulates phosphorylation of protein tyrosines, a process in which p53/56lyn kinase has been implicated. We measured the association between Fc epsilon RI and the kinase, using chemical crosslinking to stabilize their interaction. In the rat basophilic leukemia mast cell line, 3-4%, and at most 20%, of Fc epsilon RI appear to be associated with the kinase prior to aggregation, even though there is an excess of total cell lyn kinase. Aggregating the Fc epsilon RI causes three to four times more of the kinase to associate with receptors, a process requiring a prior phosphorylation step. In an in vitro assay, the lyn associated with the aggregated receptors becomes disproportionately more phosphorylated than would be predicted from the amount of lyn associated with the receptors. These and other data are consistent with a model in which aggregation of the receptor leads to its transphosphorylation by constitutively associated lyn kinase. We propose that additional molecules of this kinase are thereby recruited and that this markedly enhances transphosphorylation of tyrosine on the receptor and associated proteins, thereby initiating a cascade of further biochemical changes. This model is also consistent with data on receptors such as the clonotypic receptors on B and T lymphocytes, which share structural and functional features with Fc epsilon RI.
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