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ErbB3/HER3 does not homodimerize upon neuregulin binding at the cell surface
Author(s) -
Berger Mitchell B,
Mendrola Jeannine M,
Lemmon Mark A
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.2004.06.014
Subject(s) - erbb3 , erbb4 , neuregulin , neuregulin 1 , microbiology and biotechnology , extracellular , chimera (genetics) , receptor , chemistry , erbb , biology , kinase , signal transduction , biochemistry , receptor tyrosine kinase , gene
To understand signaling by the neuregulin (NRG) receptor ErbB3/HER3, it is important to know whether ErbB3 forms homodimers upon ligand binding. Previous biophysical studies suggest that the ErbB3 extracellular region remains monomeric when bound to NRG. We used a chimeric receptor approach to address this question in living cells, fusing the extracellular region of ErbB3 to the kinase‐active intracellular domain of ErbB1. The ErbB3/ErbB1 chimera responded to NRG only if ErbB2 was co‐expressed in the same cells, whereas an ErbB4/ErbB1 chimera responded without ErbB2. We, therefore, suggest that ErbB3 is an obligate heterodimerization partner because of its inability to homodimerize.