Characterization of the interactions between Nedd4-2, ENaC,and sgk-1 using surface plasmon resonance |
| |
Authors: | Asher Carol Sinha Indranil Garty Haim |
| |
Affiliation: | Department of Biological Chemistry, The Weizmann Institute of Science, 76100, Rehovot, Israel. |
| |
Abstract: | 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 microM range. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|