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Journal Article

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

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Camasses,  Alain
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Bogdanova,  Aliona
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Shevchenko,  Andrej
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Zachariae,  Wolfgang
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Citation

Camasses, A., Bogdanova, A., Shevchenko, A., & Zachariae, W. (2003). The CCT chaperonin promotes activation of the anaphase-promoting complex through the generation of functional Cdc20. Molecular Cell, 12(1), 87-100.


Cite as: https://hdl.handle.net/21.11116/0000-0001-12FE-D
Abstract
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.