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Updated: Aug 17, 2026

A High Resolution Method to Monitor Phosphorylation-dependent Activation of IRF3
Published on: January 24, 2016
Protein tyrosine phosphatase activity is required for IL-4 induction of IL-4 receptor alpha-chain
1Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA. hhuang@helix.nih.gov
Abstract:
To investigate the role of protein tyrosine phosphatases in IL-4Ralpha-chain expression and signaling, we first established that SHP-1, but not SHP-2, coimmunoprecipitated with anti-IL-4Ralpha chain Abs in extracts prepared from resting lymphocytes. We further observed that the protein tyrosine phosphatase inhibitors Na3VO4 and pervanadate blocked the striking induction of IL-4Ralpha-chain expression that is mediated by IL-4. However, Na3VO4 did not diminish IL-4-induced Stat6 phosphorylation nor did it block the IL-4-mediated increase in IL-4Ralpha-chain mRNA. The striking inhibition in total cellular IL-4Ralpha-chain and in cell surface IL-4 receptors was associated with an inhibition of biosynthetic labeling of IL-4Ralpha-chain after a 30- min pulse with [35S] methionine, indicating that reduction of IL-4Ralpha-chain protein resulted from either a diminished production of the receptor or a rapid degradation, possibly as a result of phosphorylation of the receptor in an early biosynthetic cellular compartment. Control of newly synthesized IL-4Ralpha-chain protein expression by phosphatase may provide a novel means to regulate IL-4 responsiveness.
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