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NEDD8 recruits E2-ubiquitin to SCF E3 ligase.

NEDD8/Rub1 is a ubiquitin (Ub)-like post-translational modifier that is covalently linked to cullin (Cul)-family proteins in a manner analogous to ubiquitylation. NEDD8 is known to enhance the ubiquitylating activity of the SCF complex (composed of Skp1, Cul-1, ROC1 and F-box protein), but the mechanistic role is largely unknown. Using an in vitro reconstituted system, we report here that NEDD8 modification of Cul-1 enhances recruitment of Ub-conjugating enzyme Ubc4 (E2) to the SCF complex (E3). This recruitment requires thioester linkage of Ub to Ubc4. Our findings indicate that the NEDD8-modifying system accelerates the formation of the E2-E3 complex, which stimulates protein polyubiquitylation.

Pubmed ID: 11483504

Authors

  • Kawakami T
  • Chiba T
  • Suzuki T
  • Iwai K
  • Yamanaka K
  • Minato N
  • Suzuki H
  • Shimbara N
  • Hidaka Y
  • Osaka F
  • Omata M
  • Tanaka K

Journal

The EMBO journal

Publication Data

August 1, 2001

Associated Grants

None

Mesh Terms

  • Anaphase-Promoting Complex-Cyclosome
  • Cell Line
  • DNA-Binding Proteins
  • Humans
  • I-kappa B Proteins
  • Ligases
  • Peptide Synthases
  • SKP Cullin F-Box Protein Ligases
  • Ubiquitin-Conjugating Enzymes
  • Ubiquitin-Protein Ligase Complexes
  • Ubiquitin-Protein Ligases
  • Ubiquitins