An open-and-shut case? Recent insights into the activation of EGF/ErbB receptors

Mol Cell. 2003 Sep;12(3):541-52. doi: 10.1016/s1097-2765(03)00350-2.


Recent crystallographic studies have provided significant new insight into how receptor tyrosine kinases from the EGF receptor or ErbB family are regulated by their growth factor ligands. EGF receptor dimerization is mediated by a unique dimerization arm, which becomes exposed only after a dramatic domain rearrangement is promoted by growth factor binding. ErbB2, a family member that has no ligand, has its dimerization arm constitutively exposed, and this explains several of its unique properties. We outline a mechanistic view of ErbB receptor homo- and heterodimerization, which suggests new approaches for interfering with these processes when they are implicated in human cancers.

Publication types

  • Review

MeSH terms

  • Animals
  • Cell Transformation, Neoplastic / metabolism
  • ErbB Receptors / metabolism*
  • Eukaryotic Cells / metabolism*
  • Growth Substances / metabolism*
  • Humans
  • Ligands
  • Models, Molecular
  • Molecular Conformation
  • Neoplasms / drug therapy
  • Neoplasms / metabolism
  • Oncogene Proteins v-erbB / metabolism*
  • Protein Structure, Tertiary


  • Growth Substances
  • Ligands
  • Oncogene Proteins v-erbB
  • ErbB Receptors