Transactivation of erbB2 by short and long isoforms of leptin receptors

Avital Eisenberg; Eva Biener; Madia Charlier; R. V. Krishnan; Jean Djiane; Brian Herman; Arieh Gertler

doi:10.1016/j.febslet.2004.03.089

Transactivation of erbB2 by short and long isoforms of leptin receptors

Avital Eisenberg, Eva Biener, Madia Charlier, R. V. Krishnan, Jean Djiane, Brian Herman, Arieh Gertler^*

^*Corresponding author for this work

Institute of Biochemistry, Food Science and Nutrition

Research output: Contribution to journal › Article › peer-review

40 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	139-142
Number of pages	4
Journal	FEBS Letters
Volume	565
Issue number	1-3
DOIs	https://doi.org/10.1016/j.febslet.2004.03.089
State	Published - 7 May 2004

Keywords

Fluorescence resonance energy transfer
Leptin
Prolactin
Receptor
erbB2

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10.1016/j.febslet.2004.03.089

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title = "Transactivation of erbB2 by short and long isoforms of leptin receptors",

abstract = "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.",

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AU - Eisenberg, Avital

AU - Biener, Eva

AU - Charlier, Madia

AU - Krishnan, R. V.

AU - Djiane, Jean

AU - Herman, Brian

AU - Gertler, Arieh

PY - 2004/5/7

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AB - 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.

KW - Fluorescence resonance energy transfer

KW - Leptin

KW - Prolactin

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Transactivation of erbB2 by short and long isoforms of leptin receptors

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Keywords

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