Journal
CELL DEATH AND DIFFERENTIATION
Volume 17, Issue 1, Pages 68-77Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/cdd.2009.84
Keywords
ubiquitylation; endocytosis; trafficking; receptor; signaling
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Funding
- NIH [DK52617, AR052647, DE16215]
- National Health and Medical Research Council [508086]
- Australian Research Council [DP0880571]
- NATIONAL INSTITUTE OF DENTAL &CRANIOFACIAL RESEARCH [P50DE016215] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [P50DK052617] Funding Source: NIH RePORTER
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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. Cell Death and Differentiation (2010) 17, 68-77; doi:10.1038/cdd.2009.84; published online 26 June 2009
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