Transactivation of erbB2 by short and long isoforms of leptin receptors

被引：34

作者：

Eisenberg, A

Biener, E

Charlier, M

Krishnan, RV

Djiane, J

Herman, B

Gertler, A

机构：

[1] Hebrew Univ Jerusalem, Fac Agr Food & Environm Qual Sci, IL-76100 Rehovot, Israel

[2] INRA, Unite Neurocrinol Mol Prise Alimentaire, F-78352 Jouy En Josas, France

[3] Univ Texas, Hlth Sci Ctr, Dept Cellular & Struct Biol, San Antonio, TX 78229 USA

来源：

FEBS LETTERS | 2004年 / 565卷 / 1-3期

基金：

以色列科学基金会;

关键词：

erbB2; leptin; prolactin; receptor; fluorescence resonance energy transfer;

D O I：

10.1016/j.febslet.2004.03.089

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：

We generated kinase-positive and kinase-negative erbB2 tagged with YFP and the long form of leptin receptor (LEPRb) tagged with CFP. Both were as active as their untagged analogs. Both short and long isoforms of leptin receptor phosphorylated and thereby activated erbB2 upon leptin binding and enhanced MAPK activity. Our results unveil a novel route by which leptin may provoke erbB2's phosphorylation and thus enhance its oncogenic potential independently of HER family ligands or its overexpression. Using FRET technology in living cells, we found no evidence of complex formation between erbB2 and prolactin or leptin receptors, indicating that the transactivation occurs through an indirect interaction. (C) 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.

引用

页码：139 / 142

页数：4

共 23 条

[1] Activation of downstream signals by the long form of the leptin receptor [J].