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

Takumi Kamura, Michael N. Conrad, Qin Yan, Ronald C. Conaway, Joan Weliky Conaway

Research output: Contribution to journalArticlepeer-review

231 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)2928-2933
Number of pages6
JournalGenes and Development
Volume13
Issue number22
DOIs
StatePublished - 1999
Externally publishedYes

Keywords

  • Cullin
  • Hrt1
  • NEDD8
  • Rbx1
  • ROC1
  • Rub1
  • SCF
  • Ubiquitin ligase
  • vonHippel-Lindau

ASJC Scopus subject areas

  • Genetics
  • Developmental Biology

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