RETRACTED: Regulation of APC activity by phosphorylation and regulatory factors (Retracted Article)

被引:119
作者
Kotani, S
Tanaka, H
Yasuda, H
Todokoro, K
机构
[1] RIKEN, Inst Phys & Chem Res, Tsukuba Life Sci Ctr, Tsukuba, Ibaraki 3050074, Japan
[2] Tokyo Univ Pharm & Life Sci, Sch Life Sci, Tokyo 1920355, Japan
关键词
anaphase-promoting complex; Cdc20; Cdh1; Mad2; phosphorylation;
D O I
10.1083/jcb.146.4.791
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Ubiquitin-dependent proteolysis of Cut2/Pds1 and Cyclin B is required for sister chromatid separation and exit from mitosis, respectively. Anaphase-promoting complex/cyclosome (APC) specifically ubiquitinates Cut2/Pds1 at metaphase-anaphase transition, and ubiquitinates Cyclin B in late mitosis and G1 phase. However, the exact regulatory mechanism of substrate-specific activation of mammalian APC with the right timing remains to be elucidated. We found that not only the binding of the activators Cdc20 and Cdh1 and the inhibitor Mad2 to APC, but also the phosphorylation of Cdc20 and Cdh1 by Cdc2-Cyclin B and that of APC by Polo-like kinase and cAMP-dependent protein kinase, regulate APC activity. The cooperation of the phosphorylation/dephosphorylation and the regulatory factors in regulation of APC activity may thus control the precise progression of mitosis.
引用
收藏
页码:791 / 800
页数:10
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