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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 |
Published version: | http://dx.doi.org/10.1016/j.biocel.2005.11.006 |
Appears in Collections: | Aurora harvest 2 Medicine publications |
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