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• W2019948850 abstract "Abstract Shc is an SH2-containing adapter protein that binds to and is phosphorylated by a large number of growth factor receptors. Phosphorylated Shc is able to interact with the Grb2-Sos complex which is responsible for mediating nucleotide exchange on Ras. We have shown previously that binding of Shc to the epidermal growth factor (EGF)-like receptor, c-ErbB-3, is through an NPXY motif (Prigent, S. A., and Gullick, W. J.(1994) EMBO J. 13, 2831−2841) shared by middle T antigen, TrkA, and EGF receptor. It has recently been reported that a region distinct from the SH2 domain is able to bind to tyrosine-phosphorylated proteins. In this paper we have used fusion proteins of various Shc domains to show that it is the N-terminal domain of Shc that is primarily responsible for binding EGF receptor and c-ErbB-3. Furthermore, by competition studies with synthetic phosphopeptides we have shown that this N-terminal domain binds to the previously identified NPXY motif." @default.
• W2019948850 created "2016-06-24" @default.
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• W2019948850 date "1995-09-01" @default.
• W2019948850 modified "2023-10-04" @default.
• W2019948850 title "Binding of Shc to the NPXY Motif Is Mediated by Its N-terminal Domain" @default.
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• W2019948850 doi "https://doi.org/10.1074/jbc.270.38.22097" @default.
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