[HTML][HTML] Identification of Trk binding sites for SHC and phosphatidylinositol 3'-kinase and formation of a multimeric signaling complex.
A Obermeier, R Lammers, KH Wiesmüller… - Journal of Biological …, 1993 - Elsevier
A Obermeier, R Lammers, KH Wiesmüller, G Jung, J Schlessinger, A Ullrich
Journal of Biological Chemistry, 1993•ElsevierPhosphotyrosine-containing synthetic peptides were used to identify the binding sites for
cellular polypeptides involved in nerve growth factor receptor/Trk-mediated signal
transduction. In vitro association of SHC and the p85 subunit of phosphatidylinositol 3'-
kinase with the Trk tyrosine kinase was prevented only by phosphorylated Y-490-and Y-751-
containing peptides, respectively. In spite of the close proximity of the p85 binding site to that
of phospholipase C gamma (Y-785), both target proteins are able to interact with the same …
cellular polypeptides involved in nerve growth factor receptor/Trk-mediated signal
transduction. In vitro association of SHC and the p85 subunit of phosphatidylinositol 3'-
kinase with the Trk tyrosine kinase was prevented only by phosphorylated Y-490-and Y-751-
containing peptides, respectively. In spite of the close proximity of the p85 binding site to that
of phospholipase C gamma (Y-785), both target proteins are able to interact with the same …
Phosphotyrosine-containing synthetic peptides were used to identify the binding sites for cellular polypeptides involved in nerve growth factor receptor/Trk-mediated signal transduction. In vitro association of SHC and the p85 subunit of phosphatidylinositol 3'-kinase with the Trk tyrosine kinase was prevented only by phosphorylated Y-490- and Y-751-containing peptides, respectively. In spite of the close proximity of the p85 binding site to that of phospholipase C gamma (Y-785), both target proteins are able to interact with the same receptor molecule simultaneously.
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