Down-Regulating Destruction: Phosphorylation Regulates the E3 Ubiquitin Ligase Nedd4-2

Peter M. Snyder^*

Department of Internal Medicine and Molecular Physiology and Biophysics, University of Iowa, Iowa City, IA 52242, USA.

Abstract: E3 ubiquitin ligases catalyze ubiquitination, which can target specific proteins for degradation. Although a growing number of E3 ubiquitin ligases and their targets have been identified, much less is known about the mechanisms that regulate their activity. A convergence of data indicate that phosphorylation regulates the binding of Nedd4-2, a HECT (homologous to the E6-AP C terminus) domain E3 ubiquitin ligase, to its target, the epithelial Na⁺ channel ENaC. Nedd4-2 phosphorylation is emerging as a central convergence point for the regulation of epithelial Na⁺ transport.

* Corresponding author. E-mail: peter-snyder{at}uiowa.edu

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