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Interferon gamma‐dependent transactivation of epidermal growth factor receptor
Author(s) -
Burova Elena,
Vassilenko Konstantin,
Dorosh Victoria,
Gonchar Ilya,
Nikolsky Nikolai
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.03.002
Subject(s) - transactivation , a431 cells , tyrosine kinase , cancer research , epidermal growth factor receptor , proto oncogene tyrosine protein kinase src , epidermal growth factor , microbiology and biotechnology , tyrosine phosphorylation , chemistry , receptor tyrosine kinase , biology , phosphorylation , signal transduction , receptor , biochemistry , oncogene , transcription factor , cell , cell cycle , gene
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.