Identification of 14-3-3ζ as an EGF receptor interacting protein

• Published in: FEBS letters Vol. 569; no. 1-3; pp. 207 - 210
• Main Authors: Oksvold, Morten P, Huitfeldt, Henrik S, Langdon, Wallace Y
• Format: Journal Article
• Language: English
• Published: Elsevier B.V 02-07-2004
• Subjects: 14-3-3; Adapter protein; Receptor tyrosine kinase; Signal transduction; 14-3-3; Receptor tyrosine kinase; Signal transduction; Adapter protein
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/j.febslet.2004.05.068

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.