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

Shusheng Wang, Ronald W. Raab, Peter J. Schatz, William B. Guggino, Min Li

Research output: Contribution to journalArticlepeer-review

Abstract

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-RB-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.

Original languageEnglish (US)
Pages (from-to)103-108
Number of pages6
JournalFEBS Letters
Volume427
Issue number1
DOIs
StatePublished - May 1 1998

Keywords

  • Cystic fibrosis
  • PDZ domain
  • PKA 1
  • Peptide display

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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