C-kinase phosphorylates the epidermal growth factor receptor and reduces its epidermal growth factor-stimulated tyrosine protein kinase activity.

作者: C Cochet , G N Gill , J Meisenhelder , J A Cooper , T Hunter

DOI: 10.1016/S0021-9258(17)43389-8

关键词:

摘要: The Ca2+- and phospholipid-dependent protein kinase (C-kinase) binds tightly in the presence of Ca2+ to purified membranes A431 human epidermoid carcinoma cells. major membrane substrate for C-kinase is epidermal growth factor (EGF) receptor. Phosphorylation EGF receptor Ca2+-dependent occurs at threonine serine residues. After tryptic digestion receptor, three phosphothreonine-containing peptides were identified. These are identical with new phosphopeptides present isolated from cells treated either tumor promoters 12-O-tetradecanoylphorbol 13-acetate or teleocidin. catalyzes phosphorylation these same sites protein. results indicate that, exposed promoters, a significant population molecules. This receptors decreased self-phosphorylation tyrosine residues both vivo vitro EGF-stimulated activity vivo.

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