Journal article
Down-regulating destruction: phosphorylation regulates the E3 ubiquitin ligase Nedd4-2
Science signaling, Vol.2(79), pp.pe41-pe41
07/14/2009
DOI: 10.1126/scisignal.279pe41
PMID: 19602703
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.
Details
- Title: Subtitle
- Down-regulating destruction: phosphorylation regulates the E3 ubiquitin ligase Nedd4-2
- Creators
- Peter M Snyder - Department of Internal Medicine and Molecular Physiology and Biophysics, University of Iowa, Iowa City, IA 52242, USA. petersnyder@uiowa.edu
- Resource Type
- Journal article
- Publication Details
- Science signaling, Vol.2(79), pp.pe41-pe41
- Publisher
- United States
- DOI
- 10.1126/scisignal.279pe41
- PMID
- 19602703
- ISSN
- 1945-0877
- eISSN
- 1937-9145
- Language
- English
- Date published
- 07/14/2009
- Academic Unit
- Molecular Physiology and Biophysics; Cardiovascular Medicine; Medicine Administration; Internal Medicine
- Record Identifier
- 9984025575502771
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