Characterization of the interactions between Nedd4-2, ENaC, and sgk-1 using surface plasmon resonance

被引:31
作者
Asher, C [1 ]
Sinha, I [1 ]
Garty, H [1 ]
机构
[1] Weizmann Inst Sci, Dept Biol Chem, IL-76100 Rehovot, Israel
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2003年 / 1612卷 / 01期
关键词
ENaC; Nedd4; sgk; WW domain; epithelial Na channel; surface plasmon resonance;
D O I
10.1016/S0005-2736(03)00083-X
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
Previous studies have characterized interactions between the ubiquitin ligase Nedd4-1 and the epithelial Na+ channel (ENaC). Such interactions control the channel cell surface expression and activity. Recently, evidence has been provided that a related protein, termed Nedd4-2, is likely to be the true physiological regulator of the channel. Unlike Nedd4-1, Nedd4-2 also interacts with the aldosterone-induced channel activating kinase sgk-1. The current study uses surface plasmon resonance to quantify the binding of the four WW domains of Nedd4-2 to synthetic peptides corresponding to the PY motifs of ENaC and sgk-1. The measurements demonstrate that WW3 and WW4 are the only Nedd4-2 domains interacting with both ENaC and sgk-1 and that their binding constants are in the 1-6 muM range. (C) 2003 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:59 / 64
页数:6
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