Phosphorylation and dephosphorylation regulate APC/Ccdh1 substrate degradation

Kobi J. Simpson-Lavy, Drora Zenvirth, Michael Brandeis*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

1 Scopus citations


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.

Original languageAmerican English
Pages (from-to)3138-3145
Number of pages8
JournalCell Cycle
Issue number19
StatePublished - 2015

Bibliographical note

Publisher Copyright:
© 2015 Taylor & Francis Group, LLC.


  • APC/C
  • Cdc14
  • Cdc5
  • Cdh1
  • Clb5
  • DNA replication
  • Dbf4
  • Exit from mitosis
  • Pds1
  • Substrate phosphorylation
  • Yeast


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