Direct interactions between NEDD8 and ubiquitin E2 conjugating enzymes upregulate cullin-based E3 ligase activity
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...
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| Veröffentlicht in: | Nature structural & molecular biology 2007-02, Vol.14 (2), p.167-168 |
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| container_title | Nature structural & molecular biology |
| container_volume | 14 |
| creator | Sakata, Eri Yamaguchi, Yoshiki Miyauchi, Yasuhiro Iwai, Kazuhiro Chiba, Tomoki Saeki, Yasushi Matsuda, Noriyuki Tanaka, Keiji Kato, Koichi |
| description | 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. |
| doi_str_mv | 10.1038/nsmb1191 |
| format | Article |
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Here we demonstrate by NMR and mutational studies that NEDD8 binds the ubiquitin E2 (UBC4), but not NEDD8 E2 (UBC12). 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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.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>17206147</pmid><doi>10.1038/nsmb1191</doi><tpages>2</tpages></addata></record> |
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| ispartof | Nature structural & molecular biology, 2007-02, Vol.14 (2), p.167-168 |
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| subjects | Binding sites Biochemistry Biological Microscopy Biomedical and Life Sciences brief-communication Carrier Proteins - chemistry Cell Cycle Proteins - chemistry Cellular biology Cullin Proteins - chemistry Gene mutations Genetic aspects Health aspects Humans Life Sciences Ligases Magnetic Resonance Spectroscopy Membrane Biology Models, Molecular Molecular biology Molecular structure Mutation NEDD8 Protein NMR Nuclear magnetic resonance Physiological aspects Polyubiquitin - chemistry Protein Binding Protein Structure SKP Cullin F-Box Protein Ligases - chemistry Ubiquitin Ubiquitin-proteasome system Ubiquitins - chemistry Ubiquitins - genetics Up-Regulation |
| title | Direct interactions between NEDD8 and ubiquitin E2 conjugating enzymes upregulate cullin-based E3 ligase activity |
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