Cdh1 degradation is mediated by APC/C-Cdh1 and SCF-Cdc4 in budding yeast.

Biochem Biophys Res Commun

Department of Biological Science, Graduate School of Integrated Science and Technology, Shizuoka University, Shizuoka, 422-8529, Japan; Department of Biological Science, Faculty of Science, Shizuoka University, Shizuoka, 422-8529, Japan. Electronic address:

Published: December 2018

AI Article Synopsis

  • Cdh1 is a tumor suppressor and a component of the anaphase-promoting complex (APC/C), with its levels downregulated in various human tumors.
  • Cdh1 degradation occurs through two main pathways: APC/C-Cdh1 and SCF-Cdc4 in yeast, both of which are influenced by its localization in the nucleus.
  • The process is regulated by Cdk1, which enhances APC/C-Cdh1 degradation, while polo kinase Cdc5 promotes SCF-Cdc4-mediated degradation, indicating multiple regulatory pathways at play.

Article Abstract

Cdh1, a substrate-recognition subunit of anaphase-promoting complex/cyclosome (APC/C), is a tumor suppressor, and it is downregulated in various tumor cells in humans. APC/C-Cdh1 is activated from late M phase to G1 phase by antagonizing Cdk1-mediated inhibitory phosphorylation. However, how Cdh1 protein levels are properly regulated is ill-defined. Here we show that Cdh1 is degraded via APC/C-Cdh1 and Skp1-Cullin1-F-box (SCF)-Cdc4 in the budding yeast Saccharomyces cerevisiae. Cdh1 degradation was promoted by forced localization of Cdh1 into the nucleus, where APC/C and SCF are present. Cdk1 promoted APC/C-Cdh1-mediated Cdh1 degradation, whereas polo kinase Cdc5 elicited SCF-Cdc4-mediated degradation. Thus, Cdh1 degradation is controlled via multiple pathways.

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http://dx.doi.org/10.1016/j.bbrc.2018.10.179DOI Listing

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