The Anaphase Promoting Complex/Cyclosome (APC/C) ubiquitin ligase activated by its G1 specific adaptor protein Cdh1 is a major regulator of the cell cycle. The APC/CCdh1 mediates degradation of dozens of proteins, however, the kinetics and requirements for their degradation are largely unknown. We demonstrate that overexpression of the constitutive active CDH1m11 mutant that is not inhibited by phosphorylation results in mitotic exit in the absence of the FEAR and MEN pathways, and DNA re-replication in the absence of Cdc7 activity. This mode of mitotic exit also reveals additional requirements for APC/CCdh1 substrate degradation, which for some substrates such as Pds1 or Clb5 is dephosphorylation, but for others such as Cdc5 is phosphorylation.
Bibliographical noteFunding Information:
This research was funded by grant BSF 2007288 from the US-Israel Binational Science Foundation, and a grant from the Israel Cancer Research Fund. K.J.S.L was a recipient of an integration fellowship from the Ministry of Adsorption.
© 2015 Taylor & Francis Group, LLC.
- DNA replication
- Exit from mitosis
- Substrate phosphorylation