title: SCF and Cullin/Ring H2-based ubiquitin ligases.
abstract: Protein degradation is deployed to modulate the steady-state abundance of proteins and to switch cellular regulatory circuits from one state to another by abrupt elimination of control proteins. In eukaryotes, the bulk of the protein degradation that occurs in the cytoplasm and nucleus is carried out by the 26S proteasome. In turn, most proteins are thought to be targeted to the 26S proteasome by covalent attachment of a multiubiquitin chain. Ubiquitination of proteins requires a multienzyme system. A key component of ubiquitination pathways, the ubiquitin ligase, controls both the specificity and timing of substrate ubiquitination. This review is focused on a conserved ubiquitin ligase complex known as SCF that plays a key role in marking a variety of regulatory proteins for destruction by the 26S proteasome.
authors.affiliation: Department of Biology, California Institute of Technology, Pasadena 91125, USA. deshaies@cco.caltech.edu
authors.forename: R J
authors.initials: RJ
authors.lastname: Deshaies
mesh_terms: D000818:Animals; D018797:Cell Cycle Proteins / Q000378:metabolism; D044842:Cullin Proteins; D006801:Humans; D010453:Peptide Synthases / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D044843:SKP Cullin F-Box Protein Ligases; D013379:Substrate Specificity; D014452:Ubiquitins
chemical_list: D018797:Cell Cycle Proteins; C100318:Cullin 1; D044842:Cullin Proteins; D014452:Ubiquitins; D044843:SKP Cullin F-Box Protein Ligases; D010453:Peptide Synthases