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• W2014705255 abstract "Ubiquitin-dependent proteolysis plays an important role in cell-cycle control [1King RW Deshaies RJ Peters JM Kirschner MW How proteolysis drives the cell cycle.Science. 1996; 274: 1652-1659Crossref PubMed Scopus (1100) Google Scholar, 2Elledge SJ Harper JW The role of protein stability in the cell cycle and cancer.Biochim Biophys Acta. 1998; 1377: 61-70PubMed Google Scholar]. In budding yeast, the protein Skp1p, the cullin-family member Cdc53p, and the F-box/WD-repeat protein Cdc4p form the SCFCdc4p ubiquitin ligase complex, which targets the cyclin-dependent kinase (Cdk) inhibitor Sic1p for proteolysis [3Mathias N Johnson SL Winey M Adams AEM Goetsch L Pringle JR et al.Cdc53p acts in concert with Cdc4p and Cdc34p to control the G1-to-S-phase transition and identifies a conserved family of proteins.Mol Biol Cell. 1996; 16: 6634-6643Google Scholar, 4Willems AR Lanker S Patton EE Craig KL Nason TF Mathias N et al.Cdc53 targets phosphorylated G1 cyclins for degradation by the ubiquitin proteolytic pathway.Cell. 1996; 86: 453-463Abstract Full Text Full Text PDF PubMed Scopus (267) Google Scholar, 5Feldman RM Correll CC Kaplan KB Deshaies RJ A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p.Cell. 1997; 91: 221-230Abstract Full Text Full Text PDF PubMed Scopus (701) Google Scholar, 6Skowyra D Craig KL Tyers M Elledge SJ Harper JW F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex.Cell. 1997; 91: 209-219Abstract Full Text Full Text PDF PubMed Scopus (1001) Google Scholar, 7Verma R Feldman RM Deshaies RJ SIC1 is ubiquitinated in vitro by a pathway that requires CDC4, CDC34, and cyclin/CDK activities.Mol Biol Cell. 1997; 8: 1427-1437Crossref PubMed Scopus (136) Google Scholar, 8Patton EE Willems AR Sa D Kuras L Thomas D Craig KL Tyers M Cdc53 is a scaffold protein for multiple Cdc34/Skp1/F-box protein complexes that regulate cell division and methionine biosynthesis in yeast.Genes Dev. 1998; 12: 692-705Crossref PubMed Scopus (232) Google Scholar]. Sic1p is recruited to the SCFCdc4p complex by binding to the WD-repeat region of Cdc4p [5Feldman RM Correll CC Kaplan KB Deshaies RJ A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p.Cell. 1997; 91: 221-230Abstract Full Text Full Text PDF PubMed Scopus (701) Google Scholar, 6Skowyra D Craig KL Tyers M Elledge SJ Harper JW F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex.Cell. 1997; 91: 209-219Abstract Full Text Full Text PDF PubMed Scopus (1001) Google Scholar], while Skp1p binds to the F-box of Cdc4p [[9]Bai C Sen P Hofmann K Ma L Goebl M Harper JW Elledge SJ SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box.Cell. 1996; 86: 263-274Abstract Full Text Full Text PDF PubMed Scopus (932) Google Scholar]. In fission yeast, two distinct Cdc4p-related proteins, Pop1p/Ste16p [10Kominami K Toda T Fission yeast WD-repeat protein pop1 regulates genome ploidy through ubiquitin-proteasome-mediated degradation of the CDK inhibitor Rum1 and the S-phase initiator Cdc18.Genes Dev. 1997; 11: 1548-1560Crossref PubMed Scopus (143) Google Scholar, 11Maekawa H Kitamura K Shimoda C The Ste16 WD-repeat protein regulates cell-cycle progression under starvation through the Rum1 protein in Schizosaccharomyces pombe.Curr Genet. 1998; 33: 29-37Crossref PubMed Scopus (18) Google Scholar] and the recently identified Sud1p/Pop2p [[12]Jallepalli PV Tien D Kelly TJ sud1(+) targets cyclin-dependent kinase-phosphorylated Cdc18 and Rum1 proteins for degradation and stops unwanted diploidization in fission yeast.Proc Natl Acad Sci USA. 1998; 95: 8159-8164Crossref PubMed Scopus (53) Google Scholar], regulate the stability of the replication initiator Cdc18p and the Cdk inhibitor Rum1p. We show here that, despite their structural and functional similarities, the pop1 and pop2 genes fail to complement each other’s deletion phenotypes, indicating that they perform non-redundant, but potentially interdependent, functions in proteolysis. Consistent with this hypothesis, Pop1p and Pop2p formed heterooligomeric complexes when overexpressed, and binding of Cdc18p to Pop2p was dependent on Pop1p. The Pop1p–Pop2p interaction was mediated by the amino-terminal domain of Pop2p which, when fused to full-length Pop1p, rescued the phenotype of a Δpop1Δpop2 double mutant. Thus, close physical proximity of two distinct F-box/WD-repeat proteins directs proteolysis mediated by the SCFPop ubiquitin ligase complex." @default.
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• W2014705255 date "1999-04-01" @default.
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• W2014705255 title "F-box/WD-repeat proteins Pop1p and Sud1p/Pop2p form complexes that bind and direct the proteolysis of Cdc18p" @default.
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• W2014705255 doi "https://doi.org/10.1016/s0960-9822(99)80165-1" @default.
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