| First Author | Wang S | Year | 1998 |
| Journal | FEBS Lett | Volume | 427 |
| Issue | 1 | Pages | 103-8 |
| PubMed ID | 9613608 | Mgi Jnum | J:47599 |
| Mgi Id | MGI:1203823 | Doi | 10.1016/s0014-5793(98)00402-5 |
| Citation | Wang S, et al. (1998) Peptide binding consensus of the NHE-RF-PDZ1 domain matches the C-terminal sequence of cystic fibrosis transmembrane conductance regulator (CFTR). FEBS Lett 427(1):103-8 |
| abstractText | 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. |
