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

doi:10.1016/S1097-2765(03)00350-2

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 journal › Review article › peer-review

672 Scopus citations

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 heterodimerization, which suggests new approaches for interfering with these processes when they are implicated in human cancers.

Original language	English (US)
Pages (from-to)	541-552
Number of pages	12
Journal	Molecular cell
Volume	12
Issue number	3
DOIs	https://doi.org/10.1016/S1097-2765(03)00350-2
State	Published - Sep 1 2003
Externally published	Yes

ASJC Scopus subject areas

Molecular Biology
Cell Biology

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10.1016/S1097-2765(03)00350-2

Cite this

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

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 heterodimerization, which suggests new approaches for interfering with these processes when they are implicated in human cancers.",

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

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T1 - An open-and-shut case? Recent insights into the activation of EGF/ErbB receptors

AU - Burgess, Antony W.

AU - Cho, Hyun Soo

AU - Eigenbrot, Charles

AU - Ferguson, Kathryn M.

AU - Garrett, Thomas P.J.

AU - Leahy, Daniel J.

AU - Lemmon, Mark A.

AU - Sliwkowski, Mark X.

AU - Ward, Colin W.

AU - Yokoyama, Shigeyuki

PY - 2003/9/1

Y1 - 2003/9/1

N2 - 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.

AB - 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.

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DO - 10.1016/S1097-2765(03)00350-2

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JO - Molecular cell

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

Abstract

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