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

Antony W. Burgess, Hyun Soo Cho, Charles Eigenbrot, Kathryn M. Ferguson, Thomas P.J. Garrett, Daniel J. Leahy, Mark A. Lemmon, Mark X. Sliwkowski, Colin W. Ward, Shigeyuki Yokoyama

Research output: Contribution to journalReview articlepeer-review

724 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)541-552
Number of pages12
JournalMolecular Cell
Issue number3
Publication statusPublished - 2003 Sept 1

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology


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