Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/23361
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Type: Journal article
Title: The ubiquitin-protein ligases Nedd4 and Nedd4-2 show similar ubiquitin-conjugating enzyme specificities
Author: Fotia, A.
Cook, D.
Kumar, S.
Citation: The International Journal of Biochemistry and Cell Biology, 2006; 38(3):472-479
Publisher: Pergamon-Elsevier Science Ltd
Issue Date: 2006
ISSN: 1357-2725
1878-5875
Abstract: Nedd4 and Nedd4-2 are closely related HECT-type ubiquitin-protein ligases (E3) implicated in the regulation of a number of proteins and pathways. Given the close homology between these E3 enzymes it would be predicted that a conserved ubiquitin-conjugating enzyme (E2) specificity exists between the two proteins. However, E2 specificities for Nedd4 and Nedd4-2 are not well established. In the present studies we aimed at clarifying the E2-specificities of Nedd4 and Nedd4-2 using in vitro ubiquitination assays. We demonstrate strong substrate ubiquitination in the presence of UbcH5b by both Nedd4 and Nedd4-2. We also found that Ube2e3, an E2 previously shown to be used by Nedd4-2, is used less efficiently than UbcH5b. Our results suggest that for optimal ubiquitination Nedd4 and Nedd4-2 require the same E2 enzymes.
Keywords: E2
E3
ubiquitination
ubiquitin-protein ligase
ubiquitin-conjugating enzyme
sodium channel
substrates
N4BP1
DOI: 10.1016/j.biocel.2005.11.006
Appears in Collections:Aurora harvest 2
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