Aurora Kinase A Interacting Protein 1 (AURKAIP1)

The deduced 199-amino acid protein contains a tandem bipartite nuclear localization signal and has a calculated molecular mass of 22 kD. Kiat et al. (2002) identified homologs of AIP in mouse and rat databases, but not in lower eukaryotic genomes such as yeast, fly, and nematode. RNA dot blot analysis detected ubiquitous AIP expression, with highest levels in heart, skeletal muscle, and testis. Epitope-tagged AIP localized to the nuclear compartment of transfected HeLa cells.Western blot analysis indicated that AIP could reduce the amount of AURKA, and proteasome inhibitors reversed the loss of AURKA. Mutation analysis identified a domain within the C terminus of AIP that mediated the interaction with AURKA and regulated AURKA proteolysis. AIP did not downregulate other cell cycle proteins examined.