| | Interferon gamma-dependent transactivation of epidermal growth factor receptorEdited by Veli-Pekka Lehto Received 13 February 2007; accepted 1 March 2007. published online 09 March 2007. Abstract The present report provides evidence that, in A431 cells, interferon γ (IFNγ) induces the rapid (within 5 min), and reversible, tyrosine phosphorylation of the epidermal growth factor receptor (EGFR). IFNγ-induced EGFR transactivation requires EGFR kinase activity, as well as activity of the Src-family tyrosine kinases and JAK2. Here, we show that IFNγ-induced STAT1 activation in A431 and HeLa cells partially depends on the kinase activity of both EGFR and Src. Furthermore, in these cells, EGFR kinase activity is essential for IFNγ-induced ERK1,2 activation. This study is the first to demonstrate that EGFR is implicated in IFNγ-dependent signaling pathways. Abbreviations: EGF, epidermal growth factor, EGFR, epidermal growth factor receptor, IFNγ, interferon gamma, IFNγR, interferon gamma receptor, JAK, Janus kinase, STAT, signal transducer and activator of transcription, TGF-α, transforming growth factor-α, HB-EGF, heparin-binding EGF like growth factor, GPCR, G-protein coupled receptor, MAPK, mitogen-activated protein kinase, ERK, extracellular signal-regulated kinase, ADAM, a disintegrin and metalloprotease, GH, growth hormone, IL, interleukine, Pyk2, proline-rich tyrosine kinase 2 Department of Intracellular Signaling and Transport, Institute of Cytology of Russian Academy of Sciences, St.-Petersburg 194064, Russia  Corresponding author. Fax: +7 812 2970341.
PII: S0014-5793(07)00251-7 doi:10.1016/j.febslet.2007.03.002 © 2007 Federation of European Biochemical Societies | |
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ABSTRACT
