The SCF(HOS/beta-TRCP)-ROC1 E3 ubiquitin ligase utilizes two distinct domains within CUL1 for substrate targeting and ubiquitin ligation

Mol Cell Biol. 2000 Feb;20(4):1382-93. doi: 10.1128/MCB.20.4.1382-1393.2000.

Abstract

We describe a purified ubiquitination system capable of rapidly catalyzing the covalent linkage of polyubiquitin chains onto a model substrate, phosphorylated IkappaBalpha. The initial ubiquitin transfer and subsequent polymerization steps of this reaction require the coordinated action of Cdc34 and the SCF(HOS/beta-TRCP)-ROC1 E3 ligase complex, comprised of four subunits (Skp1, cullin 1 [CUL1], HOS/beta-TRCP, and ROC1). Deletion analysis reveals that the N terminus of CUL1 is both necessary and sufficient for binding Skp1 but is devoid of ROC1-binding activity and, hence, is inactive in catalyzing ubiquitin ligation. Consistent with this, introduction of the N-terminal CUL1 polypeptide into cells blocks the tumor necrosis factor alpha-induced and SCF-mediated degradation of IkappaB by forming catalytically inactive complexes lacking ROC1. In contrast, the C terminus of CUL1 alone interacts with ROC1 through a region containing the cullin consensus domain, to form a complex fully active in supporting ubiquitin polymerization. These results suggest the mode of action of SCF-ROC1, where CUL1 serves as a dual-function molecule that recruits an F-box protein for substrate targeting through Skp1 at its N terminus, while the C terminus of CUL1 binds ROC1 to assemble a core ubiquitin ligase.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Anaphase-Promoting Complex-Cyclosome
  • Animals
  • Base Sequence
  • Carrier Proteins / chemistry
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Cell Cycle Proteins / chemistry
  • Cell Cycle Proteins / genetics
  • Cell Cycle Proteins / metabolism*
  • Cell Line
  • Cullin Proteins*
  • DNA-Binding Proteins / metabolism
  • HeLa Cells
  • Humans
  • I-kappa B Proteins*
  • In Vitro Techniques
  • Ligases / chemistry
  • Ligases / genetics
  • Ligases / metabolism*
  • Macromolecular Substances
  • Mice
  • Models, Biological
  • NF-KappaB Inhibitor alpha
  • Peptide Synthases / chemistry
  • Peptide Synthases / genetics
  • Peptide Synthases / metabolism*
  • Plasmids / genetics
  • Protein Structure, Tertiary
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • SKP Cullin F-Box Protein Ligases
  • Substrate Specificity
  • Transfection
  • Ubiquitin-Conjugating Enzymes
  • Ubiquitin-Protein Ligase Complexes*
  • Ubiquitin-Protein Ligases
  • Ubiquitins / metabolism*
  • beta-Transducin Repeat-Containing Proteins*

Substances

  • Carrier Proteins
  • Cell Cycle Proteins
  • Cullin 1
  • Cullin Proteins
  • DNA-Binding Proteins
  • FBXW11 protein, human
  • Fbxw1b protein, mouse
  • I-kappa B Proteins
  • Macromolecular Substances
  • NFKBIA protein, human
  • Nfkbia protein, mouse
  • Recombinant Proteins
  • Ubiquitins
  • beta-Transducin Repeat-Containing Proteins
  • NF-KappaB Inhibitor alpha
  • CDC34 protein, human
  • Ubiquitin-Conjugating Enzymes
  • Ubiquitin-Protein Ligase Complexes
  • Anaphase-Promoting Complex-Cyclosome
  • SKP Cullin F-Box Protein Ligases
  • Ubiquitin-Protein Ligases
  • Ligases
  • Peptide Synthases