CFTR function and prospects for therapy

Annu Rev Biochem. 2008;77:701-26. doi: 10.1146/annurev.biochem.75.103004.142532.

Abstract

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Anions
  • Cryoelectron Microscopy
  • Cystic Fibrosis / metabolism*
  • Cystic Fibrosis Transmembrane Conductance Regulator / metabolism
  • Cystic Fibrosis Transmembrane Conductance Regulator / physiology*
  • Endocytosis
  • Endoplasmic Reticulum / metabolism
  • Genetic Therapy / methods
  • Humans
  • Models, Biological
  • Molecular Conformation
  • Mutation
  • Protein Denaturation
  • Protein Folding
  • Salts / chemistry

Substances

  • Anions
  • Salts
  • Cystic Fibrosis Transmembrane Conductance Regulator