Molecular proximity of cystic fibrosis transmembrane conductance regulator and epithelial sodium channel assessed by fluorescence resonance energy transfer.
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.
Berdiev
Bakhrom K
BK
Department of Physiology & Biophysics, Gregory Fleming James Cystic Fibrosis Research Center, The University of Alabama at Birmingham, Birmingham, Alabama 35294-0005, USA. berdiev@uab.edu
Cormet-Boyaka
Estelle
E
Tousson
Albert
A
Qadri
Yawar J
YJ
Oosterveld-Hut
Henderika M J
HM
Hong
Jeong S
JS
Gonzales
Patricia A
PA
Fuller
Cathy M
CM
Sorscher
Eric J
EJ
Lukacs
Gergely L
GL
Benos
Dale J
DJ
D002460:Cell Line; D003550:Cystic Fibrosis / Q000235:genetics / Q000378:metabolism*; D019005:Cystic Fibrosis Transmembrane Conductance Regulator / Q000235:genetics / Q000378:metabolism*; D053503:Epithelial Sodium Channels / Q000235:genetics / Q000378:metabolism*; D031541:Fluorescence Resonance Energy Transfer; D006801:Humans; D011485:Protein Binding / Q000235:genetics
C505032:CFTR protein, human; D053503:Epithelial Sodium Channels; D019005:Cystic Fibrosis Transmembrane Conductance Regulator