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• W1979107436 startingPage "38486" @default.
• W1979107436 abstract "Stats (signal transducer and activator of transcription) are latent transcription factors that translocate from the cytoplasm to the nucleus. Constitutive activation of Stat3 alpha by upstream oncoproteins and receptor tyrosine kinases has been found in many human tumors and tumor-derived cell lines. Constitutively activated Stat3 alpha is often correlated with the activation of ErbB-2, a member of the EGFR family. To explore the involvement of ErbB-2 in the activation of Stat3 and the mechanism underlying this event, an ErbB-2 point mutant was used as a model of constitutively activated receptor. Phenylalanine mutations (Y-->F) were made in the autophosphorylation sites of the receptor, and their ability to activate Stat3 alpha was evaluated. Our results suggest that Stat3 alpha and JAK2 associates with ErbB-2 prior to phosphorylation of the receptor and that full activation of Stat3 alpha by ErbB-2 requires the participation of other non-receptor tyrosine kinases. Both Src and Jak2 kinases contribute to the activation of Stat3 alpha but Src binds to ErbB-2 only when the receptor is phosphorylated. Our results also suggest that tyrosine 1139 may be important for Src homology 2 domain association because a mutant lacking this tyrosine reduces the ability of the Src homology 2 domain to bind to ErbB-2 and significantly decreases its ability to activate Stat3 alpha." @default.
• W1979107436 created "2016-06-24" @default.
• W1979107436 creator A5030108436 @default.
• W1979107436 creator A5053123634 @default.
• W1979107436 date "2002-10-01" @default.
• W1979107436 modified "2023-10-18" @default.
• W1979107436 title "ErbB-2 Activates Stat3α in a Src- and JAK2-dependent Manner" @default.
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• W1979107436 doi "https://doi.org/10.1074/jbc.m112438200" @default.
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