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APC/CCdh1 is required for the termination of CPC activity upon mitotic exit

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Original languageEnglish
JournalJournal of Cell Science
Early online date15 Sep 2020
DOIs
Publication statusE-pub ahead of print - 15 Sep 2020

Abstract

During mitosis, the chromosomal passenger complex (CPC) ensures the faithful
transmission of the genome. CPC is composed of the enzymatic component Aurora B and
the three regulatory and targeting components Borealin, INCENP, and Survivin.
Although CPC is known to be involved in diverse mitotic events, it is still unclear how
CPC function terminates after mitosis. Here we show that Borealin is ubiquitylated by
the anaphase promoting complex/cyclosome (APC/C) and its cofactor Cdh1 and
subsequently degraded in G1 phase. Cdh1 binds to the regions within N-terminus of
Borealin that act as a non-canonical degron. Aurora-B has also been shown previously to
be degraded by the APC/CCdh1 from late mitosis to G1. Indeed, Cdh1 depletion sustains an
Aurora-B activity with stable levels of Borealin and Aurora-B throughout the cell cycle
and causes less efficiency of DNA replication after release from serum starvation.
Notably, inhibition of Aurora-B kinase activity improves the efficiency of DNA
replication in Cdh1-depleted cells. We thus propose that APC/CCdh1 terminates the CPC
activity upon mitotic exit, and thereby contributes to proper control of DNA replication.

    Research areas

  • chromosome passenger complex, borealin, ubiquitylation, aurora-B, APC/CCdh1

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