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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.
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页码:59 / 64
页数:6
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