Molecular proximity of cystic fibrosis transmembrane conductance regulator and epithelial sodium channel assessed by fluorescence resonance energy transfer

J Biol Chem. 2007 Dec 14;282(50):36481-8. doi: 10.1074/jbc.M708089200. Epub 2007 Oct 3.

Abstract

We present the evidence for a direct physical association of cystic fibrosis transmembrane conductance regulator (CFTR) and epithelial sodium channel (ENaC), two major ion channels implicated in the pathophysiology of cystic fibrosis, a devastating inherited disease. We employed fluorescence resonance energy transfer, a distance-dependent imaging technique with capability to detect molecular complexes with near angstrom resolution, to estimate the proximity of CFTR and ENaC, an essential variable for possible physical interaction to occur. Fluorescence resonance energy transfer studies were complemented with a classic biochemical approach: coimmunoprecipitation. Our results place CFTR and ENaC within reach of each other, suggestive of a direct interaction between these two proteins.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Cell Line
  • Cystic Fibrosis / genetics
  • Cystic Fibrosis / metabolism*
  • Cystic Fibrosis Transmembrane Conductance Regulator / genetics
  • Cystic Fibrosis Transmembrane Conductance Regulator / metabolism*
  • Epithelial Sodium Channels / genetics
  • Epithelial Sodium Channels / metabolism*
  • Fluorescence Resonance Energy Transfer
  • Humans
  • Protein Binding / genetics

Substances

  • CFTR protein, human
  • Epithelial Sodium Channels
  • Cystic Fibrosis Transmembrane Conductance Regulator