Aurora B kinase regulates the postmitotic endoreduplication checkpoint via phosphorylation of the retinoblastoma protein at serine 780.

The phenotypic change characteristic of Aurora B inhibition is the induction of polyploidy. Utilizing specific siRNA duplexes and a selective small molecule inhibitor (AZD1152) to inhibit Aurora B activity in tumor cells, we sought to elucidate the mechanism by which Aurora B inhibition results in polyploidy. Cells treated with AZD1152 ...
progressed through mitosis with misaligned chromosomes and exited without cytokinesis and subsequently underwent endoreduplication of DNA despite activation of a p53-dependent pseudo G1 checkpoint. Concomitant with polyploid cell formation, we observed the appearance of Rb hypophosphorylation, an event that occurred independently of cyclin-dependent kinase inhibition. We went on to discover that Aurora B directly phosphorylates Rb at serine 780 both in vitro and in vivo. This novel interaction plays a critical role in regulating the postmitotic checkpoint to prevent endoreduplication after an aberrant mitosis. Thus, we propose for the first time that Aurora B determines cellular fate after an aberrant mitosis by directly regulating the Rb tumor suppressor protein.
Mesh Terms:
Amino Acid Sequence, HCT116 Cells, Histones, Humans, Mitosis, Molecular Sequence Data, Phosphoric Acid Esters, Phosphorylation, Phosphoserine, Polyploidy, Protein Binding, Protein Kinase Inhibitors, Protein-Serine-Threonine Kinases, Quinazolines, Retinoblastoma Protein, Tumor Suppressor Protein p53
Mol. Biol. Cell
Date: Apr. 01, 2009
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