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Peptide binding consensus of the NHE-RF-PDZ1 domain matches the C-terminal sequence of cystic fibrosis transmembrane conductance regulator (CFTR).

The Na+-H+ exchanger regulatory factor (NHE-RF) is a cytoplasmic phosphoprotein that was first found to be involved in protein kinase A mediated regulation of ion transport. NHE-RF contains two distinct protein interaction PDZ domains: NHE-RF-PDZ1 and NHE-RF-PDZ2. However, their binding partners are currently unknown. Because PDZ domains usually bind to specific short linear C-terminal sequences, we have carried out affinity selection of random peptides for specific sequences that interact with the NHE-RF PDZ domains and found that NHE-RF-PDZ1 is capable of binding to the CFTR C-terminus. The specific and tight association suggests a potential regulatory role of NHE-RF in cystic fibrosis transmembrane conductance regulator (CFTR) function.

Pubmed ID: 9613608


  • Wang S
  • Raab RW
  • Schatz PJ
  • Guggino WB
  • Li M


FEBS letters

Publication Data

May 1, 1998

Associated Grants


Mesh Terms

  • Amino Acid Sequence
  • Animals
  • Consensus Sequence
  • Cystic Fibrosis Transmembrane Conductance Regulator
  • Drosophila Proteins
  • Insect Proteins
  • Mice
  • Molecular Sequence Data
  • Phosphoproteins
  • Protein Conformation
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Sodium-Hydrogen Antiporter