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- W2119294923 abstract "The Anaphase-Promoting Complex/Cyclosome (APC/C) ubiquitin ligase mediates degradation of cell cycle proteins during mitosis and G1. Cdc20/Fzy and Cdh1/Fzr are substrate-specific APC/C activators. The level of mammalian Cdh1 is high in mitosis, but it is inactive and does not bind the APC/C. We show that when Cdh1 is active in G1 and G0, its levels are considerably lower and almost all of it is APC/C associated. We demonstrate that Cdh1 is subject to APC/C-specific degradation in G1 and G0, and that this degradation depends upon two RXXL-type destruction boxes. We further demonstrate that addition of Cdh1 to Xenopus interphase extracts, which have an inactive APC/C, activates it to degrade Cdh1. These observations indicate that Cdh1 mediates its own degradation by activating the APC/C to degrade itself. Elevated levels of Cdh1 are deleterious for cell cycle progression in various organisms. This auto-regulation of Cdh1 could thus play a role in ensuring that the level of Cdh1 is reduced during G1 and G0, allowing it to be switched off at the correct time." @default.
- W2119294923 created "2016-06-24" @default.
- W2119294923 creator A5012587940 @default.
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- W2119294923 date "2004-03-18" @default.
- W2119294923 modified "2023-09-27" @default.
- W2119294923 title "Mammalian Cdh1/Fzr mediates its own degradation" @default.
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- W2119294923 doi "https://doi.org/10.1038/sj.emboj.7600149" @default.
- W2119294923 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/391060" @default.
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