title: A phosphorylation-driven ubiquitination switch for cell-cycle control.
abstract: Cellular changes in state can be dictated by complex all-or-nothing switches built from ultrasensitive protein kinase cascades, positive-feedback loops and other mechanisms. Recent work has established that phosphorylation-driven protein destruction through the SCF ubiquitin-ligase pathway can also occur in a switch-like manner. In this context, multiple phosphorylation events are used to set a threshold for substrate targeting, thereby providing a framework for understanding the inter-relationship between protein phosphorylation and ubiquitin-mediated proteolysis.
authors.forename: J Wade
authors.initials: JW
authors.lastname: Harper
mesh_terms: D017489:CDC28 Protein Kinase, S cerevisiae / Q000037:antagonists & inhibitors; D018797:Cell Cycle Proteins / Q000037:antagonists & inhibitors*; D050756:Cyclin-Dependent Kinase Inhibitor Proteins; D004791:Enzyme Inhibitors / Q000378:metabolism; D025461:Feedback, Physiological; D005656:Fungal Proteins / Q000378:metabolism; D010766:Phosphorylation; D029701:Saccharomyces cerevisiae Proteins; D014452:Ubiquitins / Q000378:metabolism / Q000502:physiology*; D015003:Yeasts
chemical_list: D018797:Cell Cycle Proteins; D050756:Cyclin-Dependent Kinase Inhibitor Proteins; D004791:Enzyme Inhibitors; D005656:Fungal Proteins; C086926:SIC1 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D014452:Ubiquitins; D017489:CDC28 Protein Kinase, S cerevisiae