The CCT chaperonin promotes activation of the anaphase-promoting complex through the generation of functional Cdc20

被引：157

作者：

Camasses, A ^{[1
]}

Bogdanova, A ^{[1
]}

Shevchenko, A ^{[1
]}

Zachariae, W ^{[1
]}

机构：

[1] Max Planck Inst Mol Cell Biol & Genet, D-01307 Dresden, Germany

来源：

MOLECULAR CELL | 2003年 / 12卷 / 01期

关键词：

D O I：

10.1016/S1097-2765(03)00244-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The WD repeat protein Cdc20 is essential for progression through mitosis because it is required to activate ubiquitin ligation by the anaphase-promoting complex (APC/C). Here we show in yeast that Cdc20 binds to the CCT chaperonin, which is known as a folding machine for actin and tubulin. The CCT is required for Cdc20's ability to bind and activate the APC/C. In vivo, CCT is essential for Cdc20-dependent cell cycle events such as sister chromatid separation and exit from mitosis. The chaperonin is also required for the function of the Cdc20-related protein Cdh1, which activates the APC/C during G1. We propose that folding of the Cdc20 family of APC/C activators is an essential and evolutionary conserved function of the CCT chaperonin.

引用

页码：87 / 100

页数：14

共 47 条

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