ArticleProceedings of the National Academy of Sciences of the United States of America1994
Dynamics of signal transduction after aggregation of cell-surface receptors: studies on the type I receptor for IgE.
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 12 papers.
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Who cites it
12 citing papers in PubMed.
- A model of cell surface receptor aggregation.Journal of mathematical biology · 2017Article
- Mast cells and company.Frontiers in immunology · 2012Article
- 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
- The SCHOOL of nature: I. Transmembrane signaling.Self/nonself · 2010Article
- Environmentally relevant metal and transition metal ions enhance Fc epsilon RI-mediated mast cell activation.Environmental health perspectives · 2003Article
- Kinetic proofreading models for cell signaling predict ways to escape kinetic proofreading.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- One lyn molecule is sufficient to initiate phosphorylation of aggregated high-affinity IgE receptors.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- Shuttling of initiating kinase between discrete aggregates of the high affinity receptor for IgE regulates the cellular response.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- 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
- Structural hierarchy in the clustering of HLA class I molecules in the plasma membrane of human lymphoblastoid cells.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Transphosphorylation as the mechanism by which the high-affinity receptor for IgE is phosphorylated upon aggregation.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- Aggregation of the high-affinity IgE receptor and enhanced activity of p53/56lyn protein-tyrosine kinase.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Many ligands stimulate cellular responses by aggregating the cell-surface receptors to which they are bound. We investigated several mechanistic questions related to aggregation of receptors by using the high-affinity receptor for IgE (Fc epsilon RI) on mast cells as a model system. We briefly exposed cells to covalently cross-linked oligomers of IgE and then added excess monomeric IgE to prevent further aggregation. Early events were examined by monitoring the phosphorylation of protein tyrosines; later events were examined by monitoring secretion. We found that aggregated receptors continue to signal both late and early events in the absence of formation of new aggregates. Additional experiments suggested that the clustered receptors undergo a dynamic process of phosphorylation and dephosphorylation. Our findings suggest that for these and related receptors that function by aggregation, the persistence of signal transduction is directly related to the intrinsic affinity of the ligand for the individual receptor.
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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.