Transcriptional and post-transcriptional regulation of Cdc20 during the spindle assembly checkpoint in S. cerevisiae

Publication date: Available online 9 February 2017
Source:Cellular Signalling
Author(s): Ruiwen Wang, Janet L. Burton, Mark J. Solomon
The anaphase-promoting complex (APC) is a ubiquitin ligase responsible for promoting the degradation of many cell cycle regulators. One of the activators and substrate-binding proteins for the APC is Cdc20. It has been shown previously that Cdc20 can promote its own degradation by the APC in normal cycling cells mainly through a cis-degradation mode (i.e. via an intramolecular mechanism). However, how Cdc20 is degraded during the spindle assembly checkpoint (SAC) is still not fully clear. In this study, we used a dual-Cdc20 system to investigate this issue and found that the cis-degradation mode is also the major pathway responsible for Cdc20 degradation during the SAC. In addition, we found that there is an inverse relationship between APC^Cdc20 activity and the transcriptional activity of the CDC20 promoter, which likely occurs through feedback regulation by APC^Cdc20 substrates, such as the cyclins Clb2 and Clb5. These findings contribute to our understanding of how the inhibition of APC^Cdc20 activity and enhanced Cdc20 degradation are required for proper spindle checkpoint arrest.



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