A Complex of Cdc4p, Skp1p, and Cdc53p/Cullin Catalyzes Ubiquitination of the Phosphorylated CDK Inhibitor Sic1p Export

@article{citeulike:2799875, abstract = {In S. cerevisiae, the G1/S transition requires Cdc4p, Cdc34p, Cdc53p, Skp1p, and the Cln/Cdc28p cyclin-dependent kinase (Cdk). These proteins are thought to promote the proteolytic inactivation of the S-phase Cdk inhibitor Sic1p. We show here that Cdc4p, Cdc53p, and Skp1p assemble into a ubiquitin ligase complex named SCFCdc4p. When mixed together, SCFCdc4p subunits, E1 enzyme, the E2 enzyme Cdc34p, and ubiquitin are sufficient to reconstitute ubiquitination of Cdk-phosphorylated Sic1p. Phosphorylated Sic1p substrate is specifically targeted for ubiquitination by binding to a Cdc4p/Skp1p subcomplex. Taken together, these data illuminate the molecular basis for the G1/S transition in budding yeast and suggest a general mechanism for phosphorylation-targeted ubiquitination in eukaryotes.}, author = {Feldman, Renny R. M. and Correll, Craig C. and Kaplan, Kenneth B. and Deshaies, Raymond J.}, citeulike-article-id = {2799875}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/S0092-8674(00)80404-3}, citeulike-linkout-1 = {http://www.sciencedirect.com/science/article/B6WSN-418PXFJ-9/1/737609961bfc49a6fbd291c8aeedffa6}, day = {17}, doi = {10.1016/S0092-8674(00)80404-3}, journal = {Cell}, keywords = {arrest, cdc4, cell, cycle, phase, regulation}, month = {October}, number = {2}, pages = {221--230}, posted-at = {2008-05-14 20:53:31}, priority = {2}, title = {A Complex of Cdc4p, Skp1p, and Cdc53p/Cullin Catalyzes Ubiquitination of the Phosphorylated CDK Inhibitor Sic1p}, url = {http://dx.doi.org/10.1016/S0092-8674(00)80404-3}, volume = {91}, year = {1997} }

TY - JOUR ID - citeulike:2799875 L3 - citeulike-article-id:2799875 N2 - In S. cerevisiae, the G1/S transition requires Cdc4p, Cdc34p, Cdc53p, Skp1p, and the Cln/Cdc28p cyclin-dependent kinase (Cdk). These proteins are thought to promote the proteolytic inactivation of the S-phase Cdk inhibitor Sic1p. We show here that Cdc4p, Cdc53p, and Skp1p assemble into a ubiquitin ligase complex named SCFCdc4p. When mixed together, SCFCdc4p subunits, E1 enzyme, the E2 enzyme Cdc34p, and ubiquitin are sufficient to reconstitute ubiquitination of Cdk-phosphorylated Sic1p. Phosphorylated Sic1p substrate is specifically targeted for ubiquitination by binding to a Cdc4p/Skp1p subcomplex. Taken together, these data illuminate the molecular basis for the G1/S transition in budding yeast and suggest a general mechanism for phosphorylation-targeted ubiquitination in eukaryotes. IS - 2 JF - Cell EP - 230 TI - A Complex of Cdc4p, Skp1p, and Cdc53p/Cullin Catalyzes Ubiquitination of the Phosphorylated CDK Inhibitor Sic1p VL - 91 SP - 221 KW - arrest KW - cdc4 KW - cell KW - cycle KW - phase KW - regulation AU - Feldman, Renny AU - Correll, Craig AU - Kaplan, Kenneth AU - Deshaies, Raymond PY - 1997/10/17/ UR - http://dx.doi.org/10.1016/S0092-8674(00)80404-3 ER -