Visintin R, Prinz S, Amon A
Whitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, MA 02142, USA.
Science. 1997 Oct 17;278(5337):460-3. doi: 10.1126/science.278.5337.460.
Proteolysis mediated by the anaphase-promoting complex (APC) triggers chromosome segregation and exit from mitosis, yet its regulation is poorly understood. The conserved Cdc20 and Cdh1 proteins were identified as limiting, substrate-specific activators of APC-dependent proteolysis. CDC20 was required for the degradation of the APC substrate Pds1 but not for that of other APC substrates, such as Clb2 and Ase1. Conversely, cdh1Delta mutants were impaired in the degradation of Ase1 and Clb2 but not in that of Pds1. Overexpression of either CDC20 or CDH1 was sufficient to induce APC-dependent proteolysis of the appropriate target in stages of the cell cycle in which substrates are normally stable.
由后期促进复合物（APC）介导的蛋白质水解触发染色体分离并促使细胞退出有丝分裂，但其调控机制仍知之甚少。保守的Cdc20和Cdh1蛋白被确定为APC依赖性蛋白质水解的限制性、底物特异性激活剂。CDC20是APC底物Pds1降解所必需的，但不是其他APC底物（如Clb2和Ase1）降解所必需的。相反，cdh1Delta突变体在Ase1和Clb2的降解中受损，但在Pds1的降解中未受损。在细胞周期中底物通常稳定的阶段，过表达CDC20或CDH1足以诱导APC对相应靶标的依赖性蛋白质水解。
