| Title |
Nedd4 and Nedd4-2: closely related ubiquitin-protein ligases with distinct physiological functions
|
|---|---|
| Published in |
Cell Death & Differentiation, June 2009
|
| DOI | 10.1038/cdd.2009.84 |
| Pubmed ID | |
| Authors | |
| Abstract |
The Nedd4 (neural precursor cell-expressed developmentally downregulated gene 4) family of ubiquitin ligases (E3s) is characterized by a distinct modular domain architecture, with each member consisting of a C2 domain, 2-4 WW domains, and a HECT-type ligase domain. Of the nine mammalian members of this family, Nedd4 and its close relative, Nedd4-2, represent the ancestral ligases with strong similarity to the yeast, Rsp5. In Saccharomyces cerevisiae Rsp5 has a key role in regulating the trafficking, sorting, and degradation of a large number of proteins in multiple cellular compartments. However, in mammals the Nedd4 family members, including Nedd4 and Nedd4-2, appear to have distinct functions, thereby suggesting that these E3s target specific proteins for ubiquitylation. In this article we focus on the biology and emerging functions of Nedd4 and Nedd4-2, and review recent in vivo studies on these E3s. |
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Mendeley demographics
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Luxembourg | 2 | 1% |
| Germany | 2 | 1% |
| United States | 1 | <1% |
| Japan | 1 | <1% |
| Chile | 1 | <1% |
| Switzerland | 1 | <1% |
| Unknown | 176 | 96% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Ph. D. Student | 53 | 29% |
| Researcher | 25 | 14% |
| Student > Bachelor | 19 | 10% |
| Student > Master | 12 | 7% |
| Student > Doctoral Student | 11 | 6% |
| Other | 27 | 15% |
| Unknown | 37 | 20% |
| Readers by discipline | Count | As % |
|---|---|---|
| Agricultural and Biological Sciences | 66 | 36% |
| Biochemistry, Genetics and Molecular Biology | 41 | 22% |
| Medicine and Dentistry | 16 | 9% |
| Neuroscience | 9 | 5% |
| Nursing and Health Professions | 3 | 2% |
| Other | 10 | 5% |
| Unknown | 39 | 21% |