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

被引:233
作者
Wang, SS
Raab, RW
Schatz, PJ
Guggino, WB
Li, M
机构
[1] Johns Hopkins Univ, Sch Med, Dept Physiol, Baltimore, MD 21205 USA
[2] Johns Hopkins Univ, Sch Med, Dept Neurosci, Baltimore, MD 21205 USA
[3] Affymax Res Inst, Dept Biol Mol, Palo Alto, CA USA
基金
美国国家卫生研究院;
关键词
cystic fibrosis; PDZ domain; peptide display; PKA;
D O I
10.1016/S0014-5793(98)00402-5
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
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. (C) 1998 Federation of European Biochemical Societies.
引用
收藏
页码:103 / 108
页数:6
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