An incomplete program of cellular tyrosine phosphorylations induced by kinase-defective epidermal growth factor receptors.
作者： Jacqueline D. Wright , Christoph W. M. Reuter , Michael J. Weber
关键词: MAPK7 、 Signal transduction 、 Immune receptor 、 Proto-oncogene tyrosine-protein kinase Src 、 Platelet-derived growth factor receptor 、 ErbB Receptors 、 Receptor tyrosine kinase 、 Biology 、 Cell biology 、 G protein-coupled receptor
摘要: Although signaling by the epidermal growth factor (EGF) receptor is thought to be dependent on tyrosine kinase activity, it clear that mitogen-activated protein (MAP) can activated receptors lacking activity. Since analysis of pathways used kinase-defective could reveal otherwise masked capabilities, we examined in detail phosphorylations and enzymes MAP pathway induced EGF receptors. Following stimulation B82L cells expressing a mutant (K721M), found ERK2 ERK1 kinases, as well MEK1 MEK2 were all activated, SHC became prominently tyrosine-phosphorylated. By contrast, failed induce detectable GAP (GTPase-activating protein), p62, JAK1, or p91STAT1, which robustly phosphorylated wild-type These data demonstrate several phosphorylations, but these represent only subset those seen with This suggests activate heterologous specificity different from receptor. We ErbB2/c-Neu enzymatic activation binding at level even greater than Thus, heterodimerization endogenous possible mechanism stimulate pathway.
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