Dynamic analysis of the epidermal growth factor (EGF) receptor-ErbB2-ErbB3 protein network by luciferase fragment complementation imaging

Jennifer L. Macdonald-Obermann, Sangeeta Adak, Ralf Landgraf, David Piwnica-Worms, Linda J. Pike

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

Background: The EGF receptor, ErbB2, and ErbB3 can interact to form dimers. Results: Analyses of these interactions show that ErbB3 interacts strongly with ErbB2 but weakly with the EGF receptor. All ErbB receptor interactions are enhanced by erlotinib and lapatinib. Conclusion: ErbB3 binds and is functionally affected by tyrosine kinase inhibitors. Significance: Tyrosine kinase inhibitors restructure the network of ErbB interactions.

Original languageEnglish
Pages (from-to)30773-30784
Number of pages12
JournalJournal of Biological Chemistry
Volume288
Issue number42
DOIs
StatePublished - Oct 18 2013

Fingerprint

Luciferases
Epidermal Growth Factor Receptor
Protein-Tyrosine Kinases
Dynamic analysis
Imaging techniques
Dimers
Proteins
lapatinib
Erlotinib Hydrochloride
ErbB Receptors

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

Dynamic analysis of the epidermal growth factor (EGF) receptor-ErbB2-ErbB3 protein network by luciferase fragment complementation imaging. / Macdonald-Obermann, Jennifer L.; Adak, Sangeeta; Landgraf, Ralf; Piwnica-Worms, David; Pike, Linda J.

In: Journal of Biological Chemistry, Vol. 288, No. 42, 18.10.2013, p. 30773-30784.

Research output: Contribution to journalArticle

Macdonald-Obermann, Jennifer L. ; Adak, Sangeeta ; Landgraf, Ralf ; Piwnica-Worms, David ; Pike, Linda J. / Dynamic analysis of the epidermal growth factor (EGF) receptor-ErbB2-ErbB3 protein network by luciferase fragment complementation imaging. In: Journal of Biological Chemistry. 2013 ; Vol. 288, No. 42. pp. 30773-30784.
@article{a4ab979314b24f0da9ec25894a3cf049,
title = "Dynamic analysis of the epidermal growth factor (EGF) receptor-ErbB2-ErbB3 protein network by luciferase fragment complementation imaging",
abstract = "Background: The EGF receptor, ErbB2, and ErbB3 can interact to form dimers. Results: Analyses of these interactions show that ErbB3 interacts strongly with ErbB2 but weakly with the EGF receptor. All ErbB receptor interactions are enhanced by erlotinib and lapatinib. Conclusion: ErbB3 binds and is functionally affected by tyrosine kinase inhibitors. Significance: Tyrosine kinase inhibitors restructure the network of ErbB interactions.",
author = "Macdonald-Obermann, {Jennifer L.} and Sangeeta Adak and Ralf Landgraf and David Piwnica-Worms and Pike, {Linda J.}",
year = "2013",
month = "10",
day = "18",
doi = "10.1074/jbc.M113.489534",
language = "English",
volume = "288",
pages = "30773--30784",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "42",

}

TY - JOUR

T1 - Dynamic analysis of the epidermal growth factor (EGF) receptor-ErbB2-ErbB3 protein network by luciferase fragment complementation imaging

AU - Macdonald-Obermann, Jennifer L.

AU - Adak, Sangeeta

AU - Landgraf, Ralf

AU - Piwnica-Worms, David

AU - Pike, Linda J.

PY - 2013/10/18

Y1 - 2013/10/18

N2 - Background: The EGF receptor, ErbB2, and ErbB3 can interact to form dimers. Results: Analyses of these interactions show that ErbB3 interacts strongly with ErbB2 but weakly with the EGF receptor. All ErbB receptor interactions are enhanced by erlotinib and lapatinib. Conclusion: ErbB3 binds and is functionally affected by tyrosine kinase inhibitors. Significance: Tyrosine kinase inhibitors restructure the network of ErbB interactions.

AB - Background: The EGF receptor, ErbB2, and ErbB3 can interact to form dimers. Results: Analyses of these interactions show that ErbB3 interacts strongly with ErbB2 but weakly with the EGF receptor. All ErbB receptor interactions are enhanced by erlotinib and lapatinib. Conclusion: ErbB3 binds and is functionally affected by tyrosine kinase inhibitors. Significance: Tyrosine kinase inhibitors restructure the network of ErbB interactions.

UR - http://www.scopus.com/inward/record.url?scp=84886907697&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84886907697&partnerID=8YFLogxK

U2 - 10.1074/jbc.M113.489534

DO - 10.1074/jbc.M113.489534

M3 - Article

C2 - 24014028

AN - SCOPUS:84886907697

VL - 288

SP - 30773

EP - 30784

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 42

ER -