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- W2051699993 abstract "Interleukin‐4 (IL‐4) triggers cellular responses by interaction with the bipartite interleukin‐4 receptor (IL‐4R). IL‐4‐responsive cells specifically endocytose IL‐4. We studied the ligand internalization properties of the human IL‐4R and analyzed the specific functions of its two subunits IL‐4Rα and γc in this process. IL‐4 mutant RY, which binds to IL‐4Rα but does not recruit γc into the receptor complex was used as a tool to show that IL‐4Rα can promote independent ligand uptake in human T cells. Internalization was limited, however, by rapid IL‐4 dissociation, suggesting that one important function of γc in IL‐4 endocytosis is to retain the ligand sufficiently long within the ternary receptor complex. We then measured IL‐4 internalization by murine Ba/F3 cells that were stably transfected with various human IL‐4R constructs. Efficient IL‐4 uptake required the cytoplasmic section of the receptor. The intracellular domains of IL‐4Rα and γc were responsible for independent endocytosis processes with distinct kinetics. IL‐4Rα‐mediated internalization resulted in long‐term intracellular maintainance of IL‐4, whereas γc directed the associated radioligand to intracellular breakdown and rapid release in the form of degraded protein. Mutants of either IL‐4R subunit deficient in Janus kinase activation were not impaired in internalization, indicating that IL‐4 endocytosis is not functionally connected to signal transduction." @default.
- W2051699993 created "2016-06-24" @default.
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- W2051699993 date "1999-10-01" @default.
- W2051699993 modified "2023-10-18" @default.
- W2051699993 title "The two subunits of the interleukin-4 receptor mediate independent and distinct patterns of ligand endocytosis" @default.
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- W2051699993 doi "https://doi.org/10.1046/j.1432-1327.1999.00773.x" @default.
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