ArticleProceedings of the National Academy of Sciences of the United States of America1992
Interaction of aggregated native and mutant IgE receptors with the cellular skeleton.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 35 citations in OpenAlex.
- Thy-1-mediated activation of rat mast cells: the role of Thy-1 membrane microdomains.Immunology · 1996Article
- Tyrosine phosphorylation of protein kinase C-delta in response to the activation of the high-affinity receptor for immunoglobulin E modifies its substrate recognition.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Cell-surface-expressed T-cell antigen-receptor zeta chain is associated with the cytoskeleton.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Multisubunit receptors in the immune system and their association with the cytoskeleton: in search of functional significance.Immunologic research · 1995Review
- 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
- Dynamics of signal transduction after aggregation of cell-surface receptors: studies on the type I receptor for IgE.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- Divalency of the monoclonal antibody 5-1-6 is required for induction of proteinuria in rats.Clinical and experimental immunology · 1993Article
- Thy-1 glycoprotein and src-like protein-tyrosine kinase p53/p56lyn are associated in large detergent-resistant complexes in rat basophilic leukemia cells.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
- Transmembrane signaling by the high-affinity IgE receptor on membrane preparations.Proceedings of the National Academy of Sciences of the United States of America · 1992Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
When aggregated, cell surface proteins become resistant to solubilization by detergents, presumably because of aggregation-induced or -stabilized interactions between the membrane protein and the cytoskeleton or plasma membrane skeleton. We genetically engineered variants of the tetrameric high-affinity receptor for IgE (Fc epsilon RI) to identify a site on its alpha, beta, or gamma chains that mediates such putative interactions. Using flow cytofluorometry, we studied rat basophilic leukemia cells, transiently transfected COS cells, and stably transfected P815 cells bearing wild-type and mutated receptors. We observed that (i) solubilization was markedly dependent on the degree of aggregation, the extent varying somewhat with the cell type and, particularly at lower levels of aggregation, with the time after addition of detergent; (ii) truncation of no single cytoplasmic domain of the alpha, beta, or gamma chains ablated the insolubilization effect; and (iii) incomplete receptors were also efficiently insolubilized by aggregation. Thus receptors consisting only of alpha and gamma chains, a "receptor" consisting of only the ectodomain of the alpha chain attached to the plasma membrane by a glycosyl-phosphatidyl inositol anchor, and "receptors" consisting only of minimally modified gamma chains were resistant to solubilization after aggregation. We conclude that no unique subunit or domain of Fc epsilon RI mediates the insolubilization phenomenon. Our results support a model in which the bridging of membrane proteins leads to their becoming nonspecifically enmeshed in a network of membrane skeletal proteins on either the outside and/or the inside of the membrane so that dissolution of the lipid bilayer becomes irrelevant.
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