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Identification of 14‐3‐3ζ as an EGF receptor interacting protein
Author(s) -
Oksvold Morten P,
Huitfeldt Henrik S,
Langdon Wallace Y
Publication year - 2004
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/j.febslet.2004.05.068
Subject(s) - epidermal growth factor , receptor , epidermal growth factor receptor , microbiology and biotechnology , serine , signal transduction , amino acid , cytoplasm , biology , cell surface receptor , mutant , biochemistry , chemistry , phosphorylation , gene
The 14‐3‐3 proteins are known to interact with a number of proteins involved in the regulation of cell signaling. Here, we describe an association of 14‐3‐3ζ with the epidermal growth factor receptor (EGFR) that is rapidly induced by EGF. The 1028‐EGFR truncated mutant which lacks the cytoplasmic tail from amino acids 1029–1186 identified the binding site for 14‐3‐3 to be between amino acid 1028 and the receptor carboxyl terminus. Mutational deletion of serine residues 1046, 1047, 1057 and 1142 did not inhibit EGF‐induced 14‐3‐3 association with the receptor. Immunofluorescence microscopy indicated an EGF‐induced co‐localization of EGFR and HA‐14‐3‐3ζ along the plasma membrane. Our finding adds to the growing complexity of EGF receptor signaling and indicates a role for 14‐3‐3 proteins in EGF receptor signaling or regulation.