Human F-box protein hCdc4 targets cyclin E for proteolysis and is mutated in a breast cancer cell line

By H. Strohmaier, C. Spruck, P. Kaiser, K. Won, O. Sangfelt, S. Reed. Nature, 2001

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Structure of the Cul1–Rbx1–Skp1–F boxSkp2 SCF ubiquitin ligase complex (2002, background): “Deregulation of SCF-dependent proteolysis can contribute to neoplastic transformation, with the loss of Cyclin E and β-catenin ubiquitination and the accelerated proteolysis of p27 Kip1 being frequent events in cancer (ref”
Systematic analysis and nomenclature of mammalian F-box proteins. (2004, background): “c-MYC and cyclin E are targeted by ago/FBXW7 in both Drosophila and mammals (Koepp et al. 2001; Moberg et al. 2001, 2004; Strohmaier et al. 2001; Tetzlaff et al. 2004; Welcker et al. 2004), and Notch is targeted by sel-10/FBXW7 in both mammals and C.”
Reading protein modifications with interaction domains (2006, background): “This leads to cyclin-E polyubiquitylation, its recruitment to a UBD on the proteasome and its degradatio”
The SCF ubiquitin ligase: insights into a molecular machine (2004, background): “Cyclin E is targeted for ubiquitylation by SCF Fbw7 through its phosphorylation at several sites by Cdk2 and glycogen-synthase kinase 3β (GSK3β”
FBW7 ubiquitin ligase: a tumour suppressor at the crossroads of cell division, growth and differentiation (2008, background): “Concurrently, two studies demonstrated that Cdc4 can function as a substrate-specificity factor for human cyclin E degradation in yeast, and that FBW7 is the human Cdc4 orthologue that catalyses phosphorylation-dependent cyclin E ubiquitylatio”