The ubiquitin-protein ligases Nedd4 and Nedd4-2 show similar ubiquitin-conjugating enzyme specificities.
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.
Mesh Terms:
Amino Acid Sequence, Animals, Endosomal Sorting Complexes Required for Transport, Molecular Sequence Data, Sequence Alignment, Substrate Specificity, Ubiquitin, Ubiquitin-Conjugating Enzymes, Ubiquitin-Protein Ligases
Amino Acid Sequence, Animals, Endosomal Sorting Complexes Required for Transport, Molecular Sequence Data, Sequence Alignment, Substrate Specificity, Ubiquitin, Ubiquitin-Conjugating Enzymes, Ubiquitin-Protein Ligases
Int. J. Biochem. Cell Biol.
Date: Mar. 01, 2006
PubMed ID: 16337426
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