CFTR function and prospects for therapy.
Mutations in the gene coding for the cystic fibrosis transmembrane conductance regulator (CFTR) epithelial anion channel cause cystic fibrosis (CF). The multidomain integral membrane glycoprotein, a member of the adenine nucleotide-binding cassette (ABC) transporter family, conserved in metazoan salt-transporting tissues, is required to control ion and fluid homeostasis on epithelial surfaces. This review considers different therapeutic strategies that have arisen from knowledge of CFTR structure and function as well as its biosynthetic processing, intracellular trafficking, and turnover.
Riordan
John R
JR
Department of Biochemistry and Biophysics, Cystic Fibrosis Treatment and Research Center, School of Medicine, University of North Carolina at Chapel Hill, NC 27599, USA. jack_riordan@med.unc.edu
D000818:Animals; D000838:Anions; D020285:Cryoelectron Microscopy; D003550:Cystic Fibrosis / Q000378:metabolism*; D019005:Cystic Fibrosis Transmembrane Conductance Regulator / Q000378:metabolism / Q000502:physiology*; D004705:Endocytosis; D004721:Endoplasmic Reticulum / Q000378:metabolism; D015316:Genetic Therapy / Q000379:methods; D006801:Humans; D008954:Models, Biological; D008968:Molecular Conformation; D009154:Mutation; D011489:Protein Denaturation; D017510:Protein Folding; D012492:Salts / Q000737:chemistry
D000838:Anions; D012492:Salts; D019005:Cystic Fibrosis Transmembrane Conductance Regulator