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

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.

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 Creators:
Camasses, Alain1, Author           
Bogdanova, Aliona1, Author           
Shevchenko, Andrej1, Author           
Zachariae, Wolfgang1, Author           
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1Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society, ou_2340692              

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 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.

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 Dates: 2003
 Publication Status: Issued
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 Identifiers: eDoc: 190444
Other: 330
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Title: Molecular Cell
Source Genre: Journal
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Pages: - Volume / Issue: 12 (1) Sequence Number: - Start / End Page: 87 - 100 Identifier: -