{Reference Type}: Journal Article
{Title}: Peptide binding consensus of the NHE-RF-PDZ1 domain matches the C-terminal sequence of cystic fibrosis transmembrane conductance regulator (CFTR).
{Author}: Wang S;Raab RW;Schatz PJ;Guggino WB;Li M;
{Journal}: FEBS Lett
{Volume}: 427
{Issue}: 1
{Year}: May 1998 1
{Factor}: 3.864
{DOI}: 10.1016/s0014-5793(98)00402-5
{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-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.