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

被引：126

作者：

Berger, MB

Mendrola, JM

Lemmon, MA ^{[1
]}

机构：

[1] Univ Penn, Sch Med, Dept Biochem & Biophys, Philadelphia, PA 19104 USA

[2] Univ Penn, Sch Med, Grad Grp Biochem & Mol Biophys, Philadelphia, PA 19104 USA

来源：

FEBS LETTERS | 2004年 / 569卷 / 1-3期

关键词：

heterodimer; epidermal growth factor; receptor; tyrosine kinase; signalling;

D O I：

10.1016/j.febslet.2004.06.014

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：332 / 336

页数：5

共 36 条

[1] Epidermal growth factor and betacellulin mediate signal transduction through co-expressed ErbB2 and ErbB3 receptors [J].