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'Rotation/twist' model for the EGF/ErbB receptor family activation
Author(s) -
Maruyama Ichiro N.
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.884.2
Subject(s) - erbb , receptor , microbiology and biotechnology , epidermal growth factor , bimolecular fluorescence complementation , receptor tyrosine kinase , epidermal growth factor receptor , growth factor receptor , chemistry , biology , signal transduction , biophysics , biochemistry , gene
The epidermal growth factor (EGF)/ErbB receptor family consists of four members, and plays pivotal roles in the development of organisms ranging from worms to humans. Furthermore, aberrant activation of the receptors is frequently implicated in a variety of human cancers. Ligand‐induced dimerization is proposed as a molecular mechanism underlying the activation of all the growth factor receptor tyrosine kinases including the ErbB receptor family. Before ligand binding, however, it remains controversial whether the receptors have a monomeric or dimeric structure. We have recently found that all the ErbB receptors have preformed, yet inactive, homo‐ and heterodimeric structures either on the cell surface or in the nucleus by bimolecular fluorescence complementation (BiFC). The spontaneous dimerization occurs in endoplasmic reticulum (ER), where ligands are unlikely to be available, before newly synthesized receptors reach the cell surface. These results are consistent with previous observations by in vivo chemical cross‐linking, cysteine disulfide bridging, FRET and FCCS. Based on current and previous results, we will propose the ?erotation/twist' model for the ErbB receptor family activation by ligand.