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- W2015339932 abstract "The cytokine interleukin-10 (IL-10) is an important regulator of immune cell function, proliferation, and survival. The IL-10 receptor (IL-10R) consists of two subunits, IL-10R1 and IL-10R2, both belonging to the class II cytokine receptor superfamily. Like other members of the cytokine receptor superfamily, IL-10R stimulation leads to activation of Jak family kinases and Stat transcription factors. To identify additional signal transduction pathways used by the IL-10R, we purified 92-kDa and 100-kDa proteins that coprecipitated with IL-10R1 from IL-10-stimulated cells. Both proteins were found to be related to the 97-kDa subunit of the regulatory component of the 26S proteasome. Subsequent studies confirmed that the IL-10R1 undergoes ligand- dependent internalization and proteasome-mediated degradation. An IL-10R1 cytoplasmic domain mutant deficient for internalization exhibited prolonged signaling through Jak1 and Stat3, reinforcing the importance of receptor internalization for signal termination." @default.
- W2015339932 created "2016-06-24" @default.
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- W2015339932 date "2006-05-01" @default.
- W2015339932 modified "2023-09-27" @default.
- W2015339932 title "Proteasome-Mediated Proteolysis of the Interleukin-10 Receptor Is Important for Signal Downregulation" @default.
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- W2015339932 doi "https://doi.org/10.1089/jir.2006.26.281" @default.
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