Aurora2 protein regulated by the anaphase-promoting complex-ubiquitin-proteasome pathway.

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Human Aurora2 was originally identified by its close homology to yeast IPL1 and fly aurora, which are key regulators of chromosome segregation and a cell cycle regulated serine/threonine protein kinase which is overexpressed in many tumor cell lines. We analyzed 100 colorectal cancer specimens for the expresssion of Aurora2 gene. The overexpression of Aurora2 gene was 62 % in primary colorectal cancers. Furthermore, we demonstrated that the Aurora2 protein is degraded rapidly after G2/M phase release in mammalian cells, (a half-life of approximately 2 h). The treatment of the cells with proteasome inhibitors blocks Aurora2 degradation. Aurora2 is polyubiquitinated in vivo and in vitro using anaphase-promoting complex (APC). These results demonstrate that Aurora2 protein js turned over through the APC-ubiquitin-proteasome pathway.We hope that the regulation of APC-ubiquitin-proteasome pathway may be useful for tumor dormancy therapy.