An open-and-shut case? Recent insights into the activation of EGF/ErbB receptors
- Author(s)
- Burgess, AW; Cho, HS; Eigenbrot, C; Ferguson, KM; Garrett, TPJ; Leahy, DJ; Lemmon, MA; Sliwkowski, MX; Ward, CW; Yokoyama, S;
- Details
- Publication Year 2003-09,Volume 12,Issue #3,Page 541-552
- Journal Title
- MOLECULAR CELL
- Publication Type
- Journal Article
- Abstract
- 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 hetero-dimerization, which suggests new approaches for interfering with these processes when they are implicated in human cancers.
- Publisher
- CELL PRESS
- Keywords
- EPIDERMAL-GROWTH-FACTOR; TYROSINE KINASE-ACTIVITY; ERBB SIGNALING NETWORK; EGF-LIKE LIGANDS; CRYSTAL-STRUCTURE; EXTRACELLULAR DOMAIN; BREAST-CANCER; FACTOR-ALPHA; BINDING DOMAIN; TRASTUZUMAB HERCEPTIN
- Publisher's Version
- https://doi.org/10.1016/S1097-2765(03)00350-2
- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 2003-09-01 12:00:00