Survivin enhances Aurora-B kinase activity and localizes Aurora-B in human cells - PubMed (original) (raw)

. 2003 Jan 3;278(1):486-90.

doi: 10.1074/jbc.M211119200. Epub 2002 Nov 4.

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• PMID: 12419797
• DOI: 10.1074/jbc.M211119200

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Survivin enhances Aurora-B kinase activity and localizes Aurora-B in human cells

Jun Chen et al. J Biol Chem. 2003.

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Abstract

Survivin, one of the most tumor-specific gene products, has been implicated in both anti-apoptosis and cytokinesis. However, the mechanism by which survivin regulates these two different processes is still elusive. Here, we show that survivin binds to the catalytic domain of Aurora-B. We demonstrate that in the presence of survivin, Aurora-B phosphorylates histone H3 much more efficiently than in the absence of survivin in a cell-free system. Furthermore, we confirm that cells lacking survivin due to survivin antisense oligonucleotide-treatment have lower Aurora-B kinase activity, whereas cells overexpressing survivin have higher Aurora-B kinase activity. We also provide evidence that depletion of survivin by survivin antisense oligonucleotide treatment causes significant reduction of endogenous phosphorylated histone H3 and mislocalization of Aurora-B. These results indicate that survivin stimulates Aurora-B kinase activity and helps correctly target Aurora-B to its substrates during the cell cycle, thus providing a mechanism as to how survivin exerts its function in human cells.

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