A unified view of cystic fibrosis transmembrane conductance regulator (CFTR) gating: Combining the allosterism of a ligand-gated channel with the enzymatic activity of an ATP-binding cassette (ABC) transporter

Academic Article

Abstract

  • The cystic fibrosis transmembrane conductance regulator (CFTR) is a unique ion channel in that its gating is coupled to an intrinsic enzymatic activity (ATP hydrolysis). This enzymatic activity derives from the evolutionary origin of CFTR as an ATP-binding cassette transporter. CFTR gating is distinct from that of a typical ligand-gated channel because its ligand (ATP) is usually consumed during the gating cycle. However, recent findings indicate that CFTR gating exhibits allosteric properties that are common to conventional ligand-gated channels (e.g. unliganded openings and constitutive mutations). Here, we provide a unified view of CFTR gating that combines the allosterism of a ligand-gated channel with its unique enzymatic activity. © 2011 by The American Society for Biochemistry and Molecular Biology, Inc.
  • Authors

    Published In

    Digital Object Identifier (doi)

    Author List

  • Kirk KL; Wang W
  • Start Page

  • 12813
  • End Page

  • 12819
  • Volume

  • 286
  • Issue

  • 15