Characterization of the interactions between Nedd4-2, ENaC, and sgk-1 using surface plasmon resonance.
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.
Mesh Terms:
Amino Acid Motifs, Amino Acid Sequence, Animals, Calcium-Binding Proteins, Endosomal Sorting Complexes Required for Transport, Epithelial Sodium Channel, Immediate-Early Proteins, Ligases, Mice, Molecular Sequence Data, Nuclear Proteins, Protein-Serine-Threonine Kinases, Recombinant Proteins, Sodium Channels, Surface Plasmon Resonance, Ubiquitin-Protein Ligases
Amino Acid Motifs, Amino Acid Sequence, Animals, Calcium-Binding Proteins, Endosomal Sorting Complexes Required for Transport, Epithelial Sodium Channel, Immediate-Early Proteins, Ligases, Mice, Molecular Sequence Data, Nuclear Proteins, Protein-Serine-Threonine Kinases, Recombinant Proteins, Sodium Channels, Surface Plasmon Resonance, Ubiquitin-Protein Ligases
Biochim. Biophys. Acta
Date: May. 02, 2003
PubMed ID: 12729930
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