Binding of Shc to the NPXY motif is mediated by its N-terminal domain

S. A. Prigent, T. S. Pillay, K. S. Ravichandran, W. J. Gullick

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29 Scopus citations

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.

Original languageEnglish
Pages (from-to)22097-22100
Number of pages4
JournalJournal of Biological Chemistry
Volume270
Issue number38
DOIs
StatePublished - 1995

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