Mitotic catenation is monitored and resolved by a PKCε-regulated pathway

Nicola Brownlow, Tanya Pike, Daniel Zicha, Lucy Collinson and Peter J. Parker ()
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Nicola Brownlow: Protein Phosphorylation Laboratory, Cancer Research UK London Research Institute
Tanya Pike: Protein Phosphorylation Laboratory, Cancer Research UK London Research Institute
Daniel Zicha: Light Microscopy, Cancer Research UK London Research Institute
Lucy Collinson: Electron Microscopy, Cancer Research UK London Research Institute
Peter J. Parker: Protein Phosphorylation Laboratory, Cancer Research UK London Research Institute

Nature Communications, 2014, vol. 5, issue 1, 1-13

Abstract: Abstract Exit from mitosis is controlled by silencing of the spindle assembly checkpoint (SAC). It is important that preceding exit, all sister chromatid pairs are correctly bioriented, and that residual catenation is resolved, permitting complete sister chromatid separation in the ensuing anaphase. Here we determine that the metaphase response to catenation in mammalian cells operates through PKCε. The PKCε-controlled pathway regulates exit from the SAC only when mitotic cells are challenged by retained catenation and this delayed exit is characterized by BubR1-high and Mad2-low kinetochores. In addition, we show that this pathway is necessary to facilitate resolution of retained catenanes in mitosis. When delayed by catenation in mitosis, inhibition of PKCε results in premature entry into anaphase with PICH-positive strands and chromosome bridging. These findings demonstrate the importance of PKCε-mediated regulation in protection from loss of chromosome integrity in cells failing to resolve catenation in G2.

Date: 2014
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DOI: 10.1038/ncomms6685

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