Evidence for epidermal growth factor (EGF)-induced intermolecular autophosphorylation of the EGF receptors in living cells.
作者： A M Honegger , A Schmidt , A Ullrich , J Schlessinger
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摘要: In response to epidermal growth factor (EGF) stimulation, the intrinsic protein tyrosine kinase of EGF receptor is activated, leading phosphorylation several cellular substrate proteins, including molecule itself. To test mechanism autophosphorylation in living cells, we established transfected cell lines coexpressing a kinase-negative point mutant (K721A) with an active lacking 63 amino acids from its carboxy terminus. The addition these cells caused by molecule, demonstrating cross-phosphorylation cells. After internalization and CD63 have separate trafficking pathways. This limits their association extent K721A CD63. coexpression together receptors same suppressed mitogenic toward as compared that express alone. presence functions negative dominant mutation suppressing receptors, probably interfering EGF-induced signal transduction. It appears, therefore, crucial events transduction occur before are separated different endocytic itineraries.
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