Interactions between NRP1 and VEGFR2 molecules in the plasma membrane

Christopher King, Daniel Wirth, Samuel Workman, Kalina A Hristova

Research output: Contribution to journalArticle

Abstract

Here we use a quantitative FRET approach, specifically developed to probe membrane protein interactions, to study the homo-association of neuropilin 1 (NRP1) in the plasma membrane, as well as its hetero-interactions with vascular endothelial growth factor receptor 2 (VEGFR2). Experiments are performed both in the absence and presence of the soluble ligand vascular endothelial growth factor A (VEGFA), which binds to both VEGFR2 and NRP1. We demonstrate the presence of homo-interactions between NRP1 molecules, as well as hetero-interactions between NRP1 and VEGFR2 molecules, in the plasma membrane. Our results underscore the complex nature of the interactions between self-associating receptors, co-receptors, and their ligands in the plasma membrane. They also highlight the need for new methodologies that capture this complexity, and the need for precise physiological measurements of local receptor surface densities in the membrane of cells. This article is part of a Special Issue entitled: Emergence of Complex Behavior in Biomembranes edited by Marjorie Longo.

Original languageEnglish (US)
JournalBiochimica et Biophysica Acta - Biomembranes
DOIs
StateAccepted/In press - Jan 1 2018

Keywords

  • Interactions
  • Membrane protein
  • Plasma membrane
  • Receptor

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Cell Biology

Fingerprint Dive into the research topics of 'Interactions between NRP1 and VEGFR2 molecules in the plasma membrane'. Together they form a unique fingerprint.

  • Cite this