ErbB3/HER3 does not homodimerize upon neuregulin binding at the cell surface.
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.[1]References
- ErbB3/HER3 does not homodimerize upon neuregulin binding at the cell surface. Berger, M.B., Mendrola, J.M., Lemmon, M.A. FEBS Lett. (2004) [Pubmed]
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