ErbB3/HER3 does not homodimerize upon neuregulin binding at the cell surface

FEBS Lett. 2004 Jul 2;569(1-3):332-6. doi: 10.1016/j.febslet.2004.06.014.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Cell Line
  • Cell Membrane
  • Cloning, Molecular
  • Dimerization
  • ErbB Receptors / metabolism
  • Humans
  • Mitogen-Activated Protein Kinases / metabolism
  • Neuregulins / metabolism*
  • Phosphorylation
  • Receptor, ErbB-3 / chemistry
  • Receptor, ErbB-3 / metabolism*
  • Recombinant Fusion Proteins / metabolism
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Spodoptera


  • Neuregulins
  • Recombinant Fusion Proteins
  • Recombinant Proteins
  • ErbB Receptors
  • Receptor, ErbB-3
  • Mitogen-Activated Protein Kinases