Wang S, Raab R W, Schatz P J, Guggino W B, Li M
Department of Physiology, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
FEBS Lett. 1998 May 1;427(1):103-8. doi: 10.1016/s0014-5793(98)00402-5.
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.
钠氢交换调节因子（NHE-RF）是一种细胞质磷蛋白，最初发现它参与蛋白激酶A介导的离子转运调节。NHE-RF包含两个不同的蛋白质相互作用PDZ结构域：NHE-RF-PDZ1和NHE-RF-PDZ2。然而，它们目前的结合伴侣尚不清楚。由于PDZ结构域通常与特定的短线性C末端序列结合，我们对与NHE-RF PDZ结构域相互作用的特定序列进行了随机肽的亲和选择，发现NHE-RF-PDZ1能够与囊性纤维化跨膜传导调节因子（CFTR）的C末端结合。这种特异性和紧密的结合表明NHE-RF在囊性纤维化跨膜传导调节因子（CFTR）功能中具有潜在的调节作用。
