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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 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.

Pubmed ID: 17206147

Authors

  • Sakata E
  • Yamaguchi Y
  • Miyauchi Y
  • Iwai K
  • Chiba T
  • Saeki Y
  • Matsuda N
  • Tanaka K
  • Kato K

Journal

Nature structural & molecular biology

Publication Data

February 5, 2007

Associated Grants

None

Mesh Terms

  • Carrier Proteins
  • Cell Cycle Proteins
  • Cullin Proteins
  • Humans
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Mutation
  • Polyubiquitin
  • Protein Binding
  • SKP Cullin F-Box Protein Ligases
  • Ubiquitins
  • Up-Regulation