Interactions between Ligand-Bound EGFR and VEGFR2

Michael D. Paul, Kalina Hristova

Research output: Contribution to journalArticlepeer-review


In this work, we put forward the provocative hypothesis that the active, ligand-bound RTK dimers from unrelated subfamilies can associate into heterooligomers with novel signaling properties. This hypothesis is based on a quantitative FRET study that monitors the interactions between EGFR and VEGFR2 in the plasma membrane of live cells in the absence of ligand, in the presence of either EGF or VEGF, and in the presence of both ligands. We show that direct interactions occur between EGFR and VEGFR2 in the absence of ligand and in the presence of the two cognate ligands. However, there are not significant heterointeractions between EGFR and VEGFR2 when only one of the ligands is present. Since RTK dimers and RTK oligomers are believed to signal differently, this finding suggests a novel mechanism for signal diversification.

Original languageEnglish (US)
Article number167006
JournalJournal of molecular biology
Issue number13
StatePublished - Jun 25 2021
Externally publishedYes


  • EGFR
  • VEGFR2
  • cell signaling
  • heterooligomers
  • receptor tyrosine kinases

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Molecular Biology


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