We describe a purified ubiquitination system capable of rapidly catalyzing the covalent
linkage of polyubiquitin chains onto a model substrate, phosphorylated IκBα. The initial …

The SCF-ROC1 ubiquitin-protein isopeptide ligase (E3) ubiquitin ligase complex targets the
ubiquitination and subsequent degradation of protein substrates required for the regulation …

SCF (Skp1· CUL1· F-box protein· ROC1) E3 ubiquitin ligase and Cdc34 E2-conjugating
enzyme catalyze polyubiquitination in a precisely regulated fashion. Here, we describe …

SCF is a ubiquitin ligase and is composed of Skp1, Cul1, F-box protein, and Roc1. The
catalytic site of the SCF is the Cul1/Roc1 complex and RING-finger protein Roc1. It was …

The Cdc34 E2 ubiquitin (Ub) conjugating enzyme catalyzes polyubiquitination of a substrate
recruited by the Skp1-Cullin 1-F-box protein-ROC1 E3 Ub ligase. Using mutagenesis …

The SCF E3 ubiquitin ligases select specific proteins for ubiquitination (and typically
destruction) by coupling variable adaptor (F box) proteins that bind protein substrates to a …

The SCF ubiquitin ligase complex regulates diverse cellular functions by ubiquitinating
numerous protein substrates. Cand1, a 120 kDa HEAT repeat protein, forms a tight complex …

ROC1 is a common component of a large family of ubiquitin E3 ligases that regulate cell
cycle progression and signal transduction pathways. Here we present evidence suggesting …

The ECS (Elongin B/C-Cul2/Cul5-SOCS-box protein) complex is a member of a family of
ubiquitin ligases that share a Cullin-Rbx module. SOCS-box proteins recruit substrates to …

The ubiquitin protein ligase SCF Skp2 is composed of Skp1, Cul1, Roc1/Rbx1 and the F‐
box protein Skp2, the substrate‐recognition subunit. Levels of Skp2 decrease as cells exit …