ArticleThe Journal of experimental medicine1995
Different roles for the Fc epsilon RI gamma chain as a function of the receptor context.
Article in The Journal of experimental medicine, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 43 citations in OpenAlex.
- NOD2 activation enhances macrophage Fcγ receptor function and may increase the efficacy of antibody therapy.Frontiers in immunology · 2024Article
- Spatial vision in insects is facilitated by shaping the dynamics of visual input through behavioral action.Frontiers in neural circuits · 2012Article
- Genome-based expression profiling study of Hunner's ulcer type interstitial cystitis: an array of 40-gene model.International urogynecology journal · 2010Article
- Article
- Cloning and sequencing of the equine and ovine high-affinity IgE receptor beta-and gamma-chain cDNA.Immunogenetics · 2003Article
- Rous-Whipple Award lecture. The biology and pathology of lymphocyte Fc receptors.The American journal of pathology · 1998Review
- Development and function of T cells in T cell antigen receptor/CD3 zeta knockout mice reconstituted with Fc epsilon RI gamma.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Systemic T cell-independent tumor immunity after transplantation of universal receptor-modified bone marrow into SCID mice.The Journal of experimental medicine · 1996Article
- Fc epsilon RI-mediated association of 6-micron beads with RBL-2H3 mast cells results in exclusion of signaling proteins from the forming phagosome and abrogation of normal downstream signaling.The Journal of cell biology · 1996Article
- Reconstitution of interactions between tyrosine kinases and the high affinity IgE receptor which are controlled by receptor clustering.The EMBO journal · 1995Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The high affinity immunoglobulin E receptor (Fc epsilon RI) and the B and T cell antigen receptors (TCR) are multimeric complexes containing subunits with cytoplasmic antigen recognition activation motifs (ARAMs). The presence of multiple motifs may be a way to amplify a single signal or provide independent activation modules. Here we have compared the signaling capacity of the same Fc epsilon RI gamma motif in the context of two different receptors, Fc epsilon RI and TCR/CD3, simultaneously reconstituted on the surface of the same zeta-deficient T cell line. Both reconstituted receptors mediate early (phosphorylation) and late (interleukin [IL]-2 release) signals. Mutation of the two tyrosine residues of ARAM gamma alters early signaling by both receptors, but the set of substrates phosphorylated via ARAM gamma is different for each receptor and is thus dependent on the receptor context. Furthermore, the mutations prevent Fc epsilon RI- but not TCR/CD3-mediated IL-2 release. These data demonstrate that ARAM gamma is necessary for allowing both receptors to phosphorylate the complete set of substrates, and that the CD3 complex, unlike the Fc epsilon RI beta chain, contains activation modules capable of compensating for the absence of a functional ARAM gamma in generating late signals such as IL-2 release.
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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.