Different epidermal growth factor (EGF) receptor ligands show distinct kinetics and biased or partial agonism for homodimer and heterodimer formation

Jennifer L. Macdonald-Obermann; Linda J. Pike

doi:10.1074/jbc.M114.586826

Different epidermal growth factor (EGF) receptor ligands show distinct kinetics and biased or partial agonism for homodimer and heterodimer formation

Jennifer L. Macdonald-Obermann
, Linda J. Pike

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

91 Scopus citations

Abstract

Background: The EGF receptor has multiple ligands that can induce different biological effects.

Results: EGF and TGFα, but not BTC or AREG, bias the EGF receptor toward heterodimer formation with ErbB2. AREG induces dimerization with different kinetics than the other ligands.

Conclusion: EGFR ligands differentially induce receptor dimerization.

Significance: This contributes to the biological differences elicited by different ligands.

Original language	English
Pages (from-to)	26178-26188
Number of pages	11
Journal	Journal of Biological Chemistry
Volume	289
Issue number	38
DOIs	https://doi.org/10.1074/jbc.M114.586826
State	Published - Sep 19 2014

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10.1074/jbc.M114.586826

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title = "Different epidermal growth factor (EGF) receptor ligands show distinct kinetics and biased or partial agonism for homodimer and heterodimer formation",

abstract = "Background: The EGF receptor has multiple ligands that can induce different biological effects.Results: EGF and TGFα, but not BTC or AREG, bias the EGF receptor toward heterodimer formation with ErbB2. AREG induces dimerization with different kinetics than the other ligands.Conclusion: EGFR ligands differentially induce receptor dimerization.Significance: This contributes to the biological differences elicited by different ligands.",

author = "Macdonald-Obermann, \{Jennifer L.\} and Pike, \{Linda J.\}",

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AU - Macdonald-Obermann, Jennifer L.

AU - Pike, Linda J.

PY - 2014/9/19

Y1 - 2014/9/19

N2 - Background: The EGF receptor has multiple ligands that can induce different biological effects.Results: EGF and TGFα, but not BTC or AREG, bias the EGF receptor toward heterodimer formation with ErbB2. AREG induces dimerization with different kinetics than the other ligands.Conclusion: EGFR ligands differentially induce receptor dimerization.Significance: This contributes to the biological differences elicited by different ligands.

AB - Background: The EGF receptor has multiple ligands that can induce different biological effects.Results: EGF and TGFα, but not BTC or AREG, bias the EGF receptor toward heterodimer formation with ErbB2. AREG induces dimerization with different kinetics than the other ligands.Conclusion: EGFR ligands differentially induce receptor dimerization.Significance: This contributes to the biological differences elicited by different ligands.

UR - https://www.scopus.com/pages/publications/84907225930

U2 - 10.1074/jbc.M114.586826

DO - 10.1074/jbc.M114.586826

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AN - SCOPUS:84907225930

SN - 0021-9258

VL - 289

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EP - 26188

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

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ER -

Different epidermal growth factor (EGF) receptor ligands show distinct kinetics and biased or partial agonism for homodimer and heterodimer formation

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