ArticleNature communications2017
Ligand-induced type II interleukin-4 receptor dimers are sustained by rapid re-association within plasma membrane microcompartments.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 37 citations in OpenAlex.
- De Novo Design and Directed Evolution Refinement of Mirror-Image Protein Binders Targeting Interleukin-4.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- In vitro and in vivo evaluation of chemically synthesized, receptor-biased interleukin-4 and photocaged variants.Science advances · 2025Article
- Transmembrane domain-driven PD-1 dimers mediate T cell inhibition.Science immunology · 2024Article
- Design of cell-type-specific hyperstable IL-4 mimetics via modular de novo scaffolds.Nature chemical biology · 2023Article
- Molecular and cellular factors determining the functional pleiotropy of cytokines.The FEBS journal · 2023Review
- Mechanism of receptor assembly via the pleiotropic adipokine Leptin.Nature structural & molecular biology · 2023Article
- Insights into receptor structure and dynamics at the surface of living cells.Nature communications · 2023Article
- Single molecule analyses reveal dynamics of Salmonella translocated effector proteins in host cell endomembranes.Nature communications · 2023Article
- Low membrane fluidity triggers lipid phase separation and protein segregation in living bacteria.The EMBO journal · 2022Article
- Competitive binding of STATs to receptor phospho-Tyr motifs accounts for altered cytokine responses.eLife · 2021Article
- Inhibition of the mitochondrial ATPase function by IF1 changes the spatiotemporal organization of ATP synthase.Biochimica et biophysica acta. Bioenergetics · 2021Article
- Engineered IL-10 variants elicit potent immunomodulatory effects at low ligand doses.Science signaling · 2020Article
- QTY Code-designed Water-soluble Fc-fusion Cytokine Receptors Bind to their Respective Ligands.QRB discovery · 2020Article
- A mesophilic cysteine-less split intein for proteinProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Article
- Report of the Signal Transduction Society Meeting 2017-Metabolism in Health and Disease.International journal of molecular sciences · 2018Article
- Mapping Determinants of Cytokine Signaling via Protein Engineering.Frontiers in immunology · 2018Review
- Tuning the Cytokine Responses: An Update on Interleukin (IL)-4 and IL-13 Receptor Complexes.Frontiers in immunology · 2018Review
Corrections and comments
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Authors and funding
16 authors at 4 institutions in 3 countries.
Funding
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.
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Registered trials
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