Trafficking and function of the cystic fibrosis transmembrane conductance regulator: a complex network of posttranslational modifications.

Academic Article

Abstract

  • Posttranslational modifications add diversity to protein function. Throughout its life cycle, the cystic fibrosis transmembrane conductance regulator (CFTR) undergoes numerous covalent posttranslational modifications (PTMs), including glycosylation, ubiquitination, sumoylation, phosphorylation, and palmitoylation. These modifications regulate key steps during protein biogenesis, such as protein folding, trafficking, stability, function, and association with protein partners and therefore may serve as targets for therapeutic manipulation. More generally, an improved understanding of molecular mechanisms that underlie CFTR PTMs may suggest novel treatment strategies for CF and perhaps other protein conformational diseases. This review provides a comprehensive summary of co- and posttranslational CFTR modifications and their significance with regard to protein biogenesis.
  • Keywords

  • cystic fibrosis, glycosylation, palmitoylation, phosphorylation, protein trafficking, ubiquitination, Animals, Cystic Fibrosis, Cystic Fibrosis Transmembrane Conductance Regulator, Glycosylation, Humans, Phosphorylation, Protein Processing, Post-Translational, Protein Stability, Protein Transport
  • Digital Object Identifier (doi)

    Author List

  • McClure ML; Barnes S; Brodsky JL; Sorscher EJ
  • Start Page

  • L719
  • End Page

  • L733
  • Volume

  • 311
  • Issue

  • 4