Identification of the two major epidermal growth factor-induced tyrosine phosphorylation sites in the microvillar core protein ezrin.
作者： J Krieg , T Hunter
DOI: 10.1016/S0021-9258(18)41769-3
关键词: Moesin 、 Radixin 、 Protein tyrosine phosphatase 、 Phosphorylation 、 Protein phosphorylation 、 Tyrosine phosphorylation 、 Biology 、 Ezrin 、 Epidermal growth factor 、 Molecular biology
摘要: In response to epidermal growth factor (EGF) the microvillar core protein ezrin is phosphorylated transiently a high level on tyrosine residues in human epidermoid carcinoma A431 cells. Here we report identification of phosphorylation sites using bacterially expressed as substrate for vitro with EGF receptor. The two major phosphotyrosine-containing peptides observed vivo were also vitro. By secondary digestions and site-directed mutagenesis tyrosines 145 353 identified phosphorylation. One sites, Tyr145, lies N-terminal region homology that common band 4.1-talin-ezrin family. This residue its vicinal amino acids are conserved throughout family members, including radixin, moesin, phosphotyrosine phosphatases, PTP H1 MEG, but not 4.1 or talin. Tyr353 localized within alpha-helical domain comparison sequences reveals this site unique ezrin.
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