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

FEBS Letters

Wang, Shusheng¹  Guggino, William B¹  Li, Min¹  Schatz, Peter J²  Raab, Ronald W² 

[1] Department of Physiology, The Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA;Department of Molecular Biology, Affymax Research Institute, Palo Alto, CA, USA

关键词: Cystic fibrosis;    PDZ domain;    Peptide display;    PKA;   

DOI  :  10.1016/S0014-5793(98)00402-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown