title: Protein destruction: adapting roles for Cks proteins.
abstract: Cks1, a subunit of cyclin-dependent kinases, has now been identified as an essential cofactor in the ubiquitination of the Cdk inhibitor p27 by the SCF(Skp2) ubiquitin ligase. This activity, which can be independent of Cdk binding, links Cks to positive growth control pathways regulating the G1/S transition and to cancer.
authors.affiliation: Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030, USA. jharper@bcm.tmc.edu
authors.forename: J W
authors.initials: JW
authors.lastname: Harper
mesh_terms: D018797:Cell Cycle Proteins / Q000378:metabolism*; D050760:Cyclin-Dependent Kinase Inhibitor p27; D018844:Cyclin-Dependent Kinases / Q000378:metabolism*; D016193:G1 Phase / Q000502:physiology*; D008025:Ligases / Q000378:metabolism*; D008954:Models, Biological; D008958:Models, Molecular; D011485:Protein Binding; D011499:Protein Processing, Post-Translational; D025521:Tumor Suppressor Proteins / Q000378:metabolism*; D025801:Ubiquitin / Q000378:metabolism*; D044767:Ubiquitin-Protein Ligases
chemical_list: D018797:Cell Cycle Proteins; D025521:Tumor Suppressor Proteins; D025801:Ubiquitin; D050760:Cyclin-Dependent Kinase Inhibitor p27; D044767:Ubiquitin-Protein Ligases; D018844:Cyclin-Dependent Kinases; C439298:p9(Cks1) protein, human; D008025:Ligases