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PubMed · 17206147

Direct interactions between NEDD8 and ubiquitin E2 conjugating enzymes upregulate cullin-based E3 ligase activity.

Eri Sakata·Yoshiki Yamaguchi·Yasuhiro Miyauchi·Kazuhiro Iwai·Tomoki Chiba·Yasushi Saeki·Noriyuki Matsuda·Keiji Tanaka·Koichi Kato
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Abstract

Although cullin-1 neddylation is crucial for the activation of SCF ubiquitin E3 ligases, the underlying mechanisms for NEDD8-mediated activation of SCF remain unclear. Here we demonstrate by NMR and mutational studies that NEDD8 binds the ubiquitin E2 (UBC4), but not NEDD8 E2 (UBC12). Our data imply that NEDD8 forms an active platform on the SCF complex for selective recruitment of ubiquitin-charged E2s in collaboration with RBX1, and thereby upregulates the E3 activity.

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Carrier ProteinsCell Cycle ProteinsCullin ProteinsHumansMagnetic Resonance SpectroscopyModels, MolecularMutationNEDD8 ProteinPolyubiquitinProtein BindingSKP Cullin F-Box Protein LigasesUbiquitinsUp-RegulationJournal ArticleResearch Support, Non-U.S. Gov't

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Eri Sakata, Yoshiki Yamaguchi, Yasuhiro Miyauchi, Kazuhiro Iwai, Tomoki Chiba, Yasushi Saeki, Noriyuki Matsuda, Keiji Tanaka, Koichi Kato. 2007-01-07. Direct interactions between NEDD8 and ubiquitin E2 conjugating enzymes upregulate cullin-based E3 ligase activity.. https://doi.org/10.1038/nsmb1191

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