Author Correction: The Aurora B specificity switch is required to protect from non-disjunction at the metaphase/anaphase transition.

An amendment to this paper has been published and can be accessed via a link at the top of the paper.

The Aurora B specificity switch is required to protect from non-disjunction at the metaphase/anaphase transition.

The Aurora B abscission checkpoint delays cytokinesis until resolution of DNA trapped in the cleavage furrow. This process involves PKCε phosphorylation of Aurora B S227. Assessing if this PKCε-Aurora B module provides a more widely exploited genome-protective control for the cell cycle, we show Aurora B phosphorylation at S227 by PKCε also occurs during mitosis.

PKCɛ switches Aurora B specificity to exit the abscission checkpoint.

The 'NoCut', or Aurora B abscission checkpoint can be activated if DNA is retained in the cleavage furrow after completion of anaphase. Checkpoint failure leads to incomplete abscission and a binucleate outcome. These phenotypes are also observed after loss of PKCɛ in transformed cell models.

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

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.

Regulation of the cytokinesis cleavage furrow by PKCε.

Cytokinesis is the final act of the cell cycle where the replicated DNA and cellular contents are finally split into two daughter cells. This process is very tightly controlled as DNA segregation errors and cytokinesis failure is commonly associated with aneuploidy and aggressive tumours. Protein kinase Cε (PKCε) is a lipid-activated serine/threonine kinase that is part of the PKC superfamily.

Novel imatinib derivatives with altered specificity between Bcr-Abl and FMS, KIT, and PDGF receptors.

Imatinib is a clinically important ATP analogue inhibitor that targets the tyrosine kinase domain of the intracellular Abl kinase and the PDGF receptor family. Imatinib has revolutionised the treatment of chronic myeloid leukaemia, which is caused by the oncogene Bcr-Abl and certain solid tumours that harbor oncogenic mutations of the PDGF receptor family. As a leading kinase inhibitor, imatinib also provides an excellent model system to investigate how changes in drug design impact biological activity, which is an important consideration for rational drug design.

Protein kinase C epsilon in cell division: control of abscission.

Cell division requires the separation and partitioning of sister chromatids to opposite ends of the cell before an actomyosin ring contracts the membrane in between during cytokinesis. The final irreversible step occurs during abscission when the ring breaks down and the membrane is sealed in its place. The physical mechanics of contraction depend on RhoA, which is stimulated by a centralspindlin complex around the cell equator.