Possible involvement of Shc in IL-4-induced germline epsilon transcription in a human B cell line.

The IL-4Ralpha contains the I4R motif which binds to the phosphotyrosine binding domain of several adaptor proteins, including IRS-1/2 and Shc. Although the involvement of IRS-1/2 in IL-4-induced PI3-kinase activation is known, there is little information on the role of Shc in IL-4 signaling. In this study, we found the ...
preferential utilization of Shc by the IL-4Ralpha in a human Burkitt's B lymphoma cell line, DND39. IL-4 induced the association of tyrosine-phosphorylated Shc with the IL-4Ralpha, whereas no detectable tyrosine phosphorylation of IRS-1 or IRS-2 was induced. IL-4-induced germline epsilon promoter activation was enhanced by overexpression of Shc and was inhibited by truncated Shc lacking the collagen-homologous domain. We further found the association of Shc with PLCgamma1. Although direct tyrosine phosphorylation of PLCgamma1 was not detectable, the amount of PLCgamma1 coprecipitable with anti-phosphotyrosine was increased after IL-4 stimulation. These results suggest that Shc can function as an adaptor protein of the IL-4Ralpha and mediate the germline epsilon transcription.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Adaptor Proteins, Vesicular Transport, B-Lymphocytes, Burkitt Lymphoma, Humans, Insulin Receptor Substrate Proteins, Interleukin-4, Intracellular Signaling Peptides and Proteins, Isoenzymes, Phospholipase C gamma, Phosphoproteins, Phosphorylation, Proteins, Receptors, Interleukin-4, Shc Signaling Adaptor Proteins, Signal Transduction, Transcription, Genetic, Tumor Cells, Cultured, Type C Phospholipases, Tyrosine
Biochem. Biophys. Res. Commun.
Date: Feb. 05, 2000
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