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Epidermal growth factor induces protein tyrosine phosphorylation and association of p190 with ras‐GTP‐ase activating protein in Caco‐2 cells
Author(s) -
Auricchio Alberto,
Domenico Marina di,
Castoria Gabriella,
Bilancio Antonio,
Migliaccio Antimo
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00987-2
Subject(s) - tyrosine phosphorylation , epidermal growth factor , phosphorylation , tyrosine kinase , microbiology and biotechnology , tyrosine , biology , receptor tyrosine kinase , protein tyrosine phosphatase , grb2 , platelet derived growth factor receptor , protein phosphorylation , sh2 domain , chemistry , growth factor , protein kinase a , biochemistry , signal transduction , receptor
Epidermal growth factor (EGF) modulates several functions of human enterocytes. We report that this growth factor induces strong tyrosine phosphorylation stimulation of its receptor and several putative substrates of the receptor intrinsic kinase including c‐erb B2 in proliferating human colon carcinoma cells (Caco‐2). In addition EGF induces stable association of the GTP‐ase activating protein of p21 ras to the p190 protein and to a 62 mol.wt. tyrosine‐phosphorylated protein. This association is probably consequent to EGF stimulation of protein tyrosine phosphorylation and could coordinate progression through cell cycle with polarity, cell—cell interactions and cell mobility.