Revisiting a controversy: The effect of EGF on EGFR dimer stability

Deo R. Singh, Christopher King, Matt Salotto, Kalina Hristova

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


EGFR is a receptor tyrosine kinase that plays a critical role in cell proliferation, differentiation, survival and migration. Its activating ligand, EGF, has long been believed to stabilize the EGFR dimer. Two research studies aimed at quantitative measurements of EGFR dimerization, however, have led to contradicting conclusions and have questioned this view. Given the controversy, here we sought to measure the dimerization of EGFR in the absence and in the presence of saturating EGF concentrations, and to tease out the effect of ligand on dimer stability, using a FRET-based quantitative method. Our measurements show that the dissociation constant is decreased ~150 times due to ligand binding, indicative of significant dimer stabilization. In addition, our measurements demonstrate that EGF binding induces a conformational change in the EGFR dimer.

Original languageEnglish (US)
Article number183015
JournalBiochimica et Biophysica Acta - Biomembranes
Issue number1
StatePublished - Jan 1 2020


  • Dimer stability
  • EGF
  • EGFR
  • Receptor tyrosine kinase
  • Thermodynamics

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology


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