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lüll Mechanisms and regulation of the degradation of cyclin B Hershko APhilos Trans R Soc Lond B Biol Sci 1999[Sep]; 354 (1389): 1571-5; discussion 1575-6The degradation of the cyclin B subunit of protein kinase Cdk1/cyclin B is required for inactivation of the kinase and exit from mitosis. Cyclin B is degraded by the ubiquitin pathway, a system involved in most selective protein degradation in eukaryotic cells. In this pathway, proteins are targeted for degradation by ligation to ubiquitin, a process carried out by the sequential action of three enzymes: the ubiquitin-activating enzyme E1, a ubiquitin-carrier protein E2 and a ubiquitin-protein ligase E3. In the system responsible for cyclin B degradation, the E3-like function is carried out by a large complex called cyclosome or anaphase-promoting complex (APC). In the early embryonic cell cycles, the cyclosome is inactive in the interphase, but becomes active at the end of mitosis. Activation requires phosphorylation of the cyclosome/APC by protein kinase Cdk1/cyclin B. The lag kinetics of cyclosome activation may be explained by Suc1-assisted multiple phosphorylations of partly phosphorylated complex. The presence of a Fizzy/Cdc20-like protein is necessary for maximal activity of the mitotic form of cyclosome/APC in cyclin-ubiquitin ligation.|*Ubiquitin-Protein Ligase Complexes[MESH]|Anaphase-Promoting Complex-Cyclosome[MESH]|Animals[MESH]|Cell Cycle[MESH]|Cell Cycle Proteins/metabolism[MESH]|Cyclin B/*metabolism[MESH]|Drosophila[MESH]|Drosophila Proteins[MESH]|Ligases/*metabolism[MESH]|Ubiquitin-Protein Ligases[MESH]|Xenopus[MESH] |