Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10872633 | FEBS Letters | 2007 | 6 Pages |
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.
Keywords
GPCRIFNγHB-EGFEGFRPYK2TransactivationTgf-αERKEGFIFNγRJanus kinaseG-protein coupled receptorMAPKStat1ADAMSTATinterleukinetransforming growth factor-αa disintegrin and metalloproteaseproline-rich tyrosine kinase 2epidermal growth factorTyrosine phosphorylationSignal transducer and activator of transcriptionGrowth hormonemitogen-activated protein kinaseJAKextracellular signal-regulated kinaseInterferon gammaEpidermal growth factor receptorInterferon gamma receptor
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Authors
Elena Burova, Konstantin Vassilenko, Victoria Dorosh, Ilya Gonchar, Nikolai Nikolsky,