Premium
Signal Transduction Using an Artificial Receptor System that Undergoes Dimerization Upon Addition of a Bivalent Leucine‐Zipper Ligand
Author(s) -
Nakase Ikuhiko,
Okumura Shinya,
Tanaka Gen,
Osaki Katsuhiro,
Imanishi Miki,
Futaki Shiroh
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201201805
Subject(s) - leucine zipper , bzip domain , zipper , bivalent (engine) , transmembrane domain , chemistry , receptor , transmembrane protein , signal transduction , biophysics , basic helix loop helix leucine zipper transcription factors , phosphorylation , microbiology and biotechnology , biochemistry , transcription factor , biology , dna binding protein , organic chemistry , algorithm , computer science , metal , gene
Examine your zipper : An artificial receptor system composed of an extracellular leucine‐zipper domain (red helices) fused to the transmembrane and cytoplasmic domains of the epidermal growth factor receptor (EGFR) is shown (see scheme). Dimerization and activation of the receptor is induced by a bivalent leucine‐zipper ligand (blue helices), leading to phosphorylation of the cytoplasmic domain of the receptor, and eliciting a signaling cascade.