Matches in SemOpenAlex for { <https://semopenalex.org/work/W2734654295> ?p ?o ?g. }
- W2734654295 abstract "Abstract The spatiotemporal organization of cytokine receptors in the plasma membrane is still debated with models ranging from ligand-independent receptor pre-dimerization to ligand-induced receptor dimerization occurring only after receptor uptake into endosomes. Here, we explore the molecular and cellular determinants governing the assembly of the type II interleukin-4 receptor, taking advantage of various agonists binding the receptor subunits with different affinities and rate constants. Quantitative kinetic studies using artificial membranes confirm that receptor dimerization is governed by the two-dimensional ligand–receptor interactions and identify a critical role of the transmembrane domain in receptor dimerization. Single molecule localization microscopy at physiological cell surface expression levels, however, reveals efficient ligand-induced receptor dimerization by all ligands, largely independent of receptor binding affinities, in line with the similar STAT6 activation potencies observed for all IL-4 variants. Detailed spatiotemporal analyses suggest that kinetic trapping of receptor dimers in actin-dependent microcompartments sustains robust receptor dimerization and signalling." @default.
- W2734654295 created "2017-07-21" @default.
- W2734654295 creator A5004011148 @default.
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- W2734654295 creator A5087389589 @default.
- W2734654295 creator A5090005733 @default.
- W2734654295 date "2017-07-14" @default.
- W2734654295 modified "2023-09-23" @default.
- W2734654295 title "Ligand-induced type II interleukin-4 receptor dimers are sustained by rapid re-association within plasma membrane microcompartments" @default.
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