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Sci. Signal., 14 July 2009
Vol. 2, Issue 79, p. pe41
[DOI: 10.1126/scisignal.279pe41]
PERSPECTIVES
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.
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EDITORS' CHOICE
Elizabeth M. Adler (14 October 2008) Sci. Signal.1 (41), ec359.
[DOI: 10.1126/scisignal.141ec359] |Abstract »
REVIEWS
Hans Häcker and Michael Karin (17 October 2006) Sci. STKE2006 (357), re13.
[DOI: 10.1126/stke.3572006re13] |Gloss »|Abstract »|Full Text »|PDF »
REVIEWS
Florian Lang and Philip Cohen (13 November 2001) Sci. STKE2001 (108), re17.
[DOI: 10.1126/scisignal.1082001re17] |Gloss »|Abstract »|Full Text »|PDF »
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