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

Biomedical Engineering

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 (US)
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 - May 7 2004

Bibliographical note

Funding Information:
This work was supported by the Binational USA – Israel Science Foundation (Grant No. 2000115) to AG and BH. We thank Dr. Y. Yarden from the Weizmann Institute, Rehovot, Israel for the plasmids encoding erbB2 and KN erbB2 and reading this manuscript, Dr. C. Bjorbaek from Harvard Medical School, Boston, MA for the plasmids encoding mouse LEPRs and Ms. Nathalie Daniel for the help in bioassay of LEPRb-CFP.

Keywords

Fluorescence resonance energy transfer
Leptin
Prolactin
Receptor
erbB2

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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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author = "Avital Eisenberg and Eva Biener and Madia Charlier and Krishnan, {R. V.} and Jean Djiane and Brian Herman and Arieh Gertler",

note = "Funding Information: This work was supported by the Binational USA – Israel Science Foundation (Grant No. 2000115) to AG and BH. We thank Dr. Y. Yarden from the Weizmann Institute, Rehovot, Israel for the plasmids encoding erbB2 and KN erbB2 and reading this manuscript, Dr. C. Bjorbaek from Harvard Medical School, Boston, MA for the plasmids encoding mouse LEPRs and Ms. Nathalie Daniel for the help in bioassay of LEPRb-CFP.",

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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

N1 - Funding Information: This work was supported by the Binational USA – Israel Science Foundation (Grant No. 2000115) to AG and BH. We thank Dr. Y. Yarden from the Weizmann Institute, Rehovot, Israel for the plasmids encoding erbB2 and KN erbB2 and reading this manuscript, Dr. C. Bjorbaek from Harvard Medical School, Boston, MA for the plasmids encoding mouse LEPRs and Ms. Nathalie Daniel for the help in bioassay of LEPRb-CFP.

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N2 - 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.

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

KW - Receptor

KW - erbB2

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Transactivation of erbB2 by short and long isoforms of leptin receptors

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Bibliographical note

Keywords

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