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Accessory protein facilitated CFTR-CFTR interaction, a molecular mechanism to potentiate the chloride channel activity.

The cystic fibrosis transmembrane conductance regulator (CFTR) gene encodes a chloride channel protein that belongs to the superfamily of ATP binding cassette (ABC) transporters. Phosphorylation by protein kinase A in the presence of ATP activates the CFTR-mediated chloride conductance of the apical membranes. We have identified a novel hydrophilic CFTR binding protein, CAP70, which is also concentrated on the apical surfaces. CAP70 consists of four PDZ domains, three of which are capable of binding to the CFTR C terminus. Linking at least two CFTR molecules via cytoplasmic C-terminal binding by either multivalent CAP70 or a bivalent monoclonal antibody potentiates the CFTR chloride channel activity. Thus, the CFTR channel can be switched to a more active conducting state via a modification of intermolecular CFTR-CFTR contact that is enhanced by an accessory protein.

Pubmed ID: 11051556


  • Wang S
  • Yue H
  • Derin RB
  • Guggino WB
  • Li M



Publication Data

September 29, 2000

Associated Grants


Mesh Terms

  • Amino Acid Sequence
  • Animals
  • Carrier Proteins
  • Cell Extracts
  • Cell Membrane
  • Cystic Fibrosis Transmembrane Conductance Regulator
  • Intestine, Small
  • Kidney
  • Membrane Proteins
  • Mice
  • Models, Biological
  • Molecular Sequence Data
  • Protein Structure, Tertiary