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Keywords :
Transfection; Receptors, Interleukin; Receptors, Cytokine; Proteins; Protein-Tyrosine Kinases; Protein Tyrosine Phosphatases; Protein Tyrosine Phosphatase, Non-Receptor Type 6; Protein Tyrosine Phosphatase, Non-Receptor Type 11; Peptides; Receptors, Interleukin-5; Receptors, OSM-LIF; Receptors, Oncostatin M; Transcription Factors; Trans-Activators; Tetradecanoylphorbol Acetate; Suppressor of Cytokine Signaling Proteins; STAT3 Transcription Factor; STAT1 Transcription Factor; Repressor Proteins; Recombinant Fusion Proteins; Oncostatin M; Mitogen-Activated Protein Kinases; Enzyme Activation; Dimerization; DNA-Binding Proteins; Cytokine Receptor gp130; Cell Line; Binding Sites; Antigens, CD; Animals; Growth Inhibitors; Humans; Interleukin-5; Membrane Glycoproteins; MAP Kinase Signaling System; Lymphokines; Leukemia Inhibitory Factor Receptor alpha Subunit; Leukemia Inhibitory Factor; Janus Kinase 1; Intracellular Signaling Peptides and Proteins; Interleukin-6; Amino Acid Motifs
Abstract :
[en] Prior activation of mitogen-activated protein kinases by phorbol 13-myristate 12-acetate (PMA) results in an inhibition of interleukin (IL)-6-induced activation of the Janus kinase/signal transducer and activator of transcription (STAT) signaling pathway which is most likely mediated by the induction of suppressor of cytokine signaling-3 and requires the specific SHP2 binding site Y759 of the IL-6 signal transducer gp130. In this study, we demonstrate that PMA inhibits STAT activation by IL-6 and the related cytokine leukemia inhibitory factor (LIF) but not by oncostatin M (OSM). Since the LIF receptor also contains an SHP2 recruitment site whereas the OSM receptor lacks such a module, we propose that two SHP2 binding modules within a homo- or heterodimeric receptor are necessary to mediate the PMA inhibitory effect.
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