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The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2.

The RING-H2 finger protein Rbx1 is a subunit of the related SCF (Skp1-Cdc53/Cul1-F-box protein) and von Hippel-Lindau (VHL) tumor suppressor (elongin BC-Cul2-VHL) E3 ubiquitin ligase complexes, where it functions as a component of Cdc53/Rbx1 and Cul2/Rbx1 modules that activate ubiquitination of target proteins by the E2 ubiquitin-conjugating enzymes Cdc34 and Ubc5. Here we demonstrate that the Cdc53/Rbx1 and Cul2/Rbx1 modules also activate conjugation of the ubiquitin-like protein Rub1 to Cdc53 and Cul2 by the dedicated E2 Rub1 conjugating enzyme Ubc12. Our findings identify Rbx1 as a common component of enzyme systems responsible for ubiquitin and Rub1 modification of target proteins.

Pubmed ID: 10579999

Authors

  • Kamura T
  • Conrad MN
  • Yan Q
  • Conaway RC
  • Conaway JW

Journal

Genes & development

Publication Data

November 15, 1999

Associated Grants

  • Agency: NIGMS NIH HHS, Id: 2 ROI GM41628

Mesh Terms

  • Amino Acid Sequence
  • Carrier Proteins
  • Cell Cycle Proteins
  • Cullin Proteins
  • Fungal Proteins
  • Ligases
  • Macromolecular Substances
  • Molecular Sequence Data
  • Peptide Synthases
  • Protein Processing, Post-Translational
  • Proteins
  • Recombinant Fusion Proteins
  • SKP Cullin F-Box Protein Ligases
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Tumor Suppressor Proteins
  • Ubiquitin-Protein Ligases
  • Ubiquitins
  • Von Hippel-Lindau Tumor Suppressor Protein
  • Zinc