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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Aurora-B associated protein phosphatases as negative regulators of kinase activation.

The human serine/threonine kinase Aurora-B is structurally related to the protein kinase Ipl1p from S cerevisiae and aurora from Drosophila melanogaster, which are key regulators of mitosis. The present study shows that human Aurora-B is activated by okadaic acid and forms complexes with the protein serine/threonine phosphatase type 1 (PP1) or PP2A, but not with PP5. These data identified Aurora-B associated protein phosphatases as negative regulators of kinase activation. We then used a series of substrates based on a histone H3 phosphorylation site (residues 5-15) to determine the substrate specificity of human Aurora-B. We found that this enzyme is an arginine-directed kinase that can phosphorylate histone H3 at serines 10 and 28 in vitro, suggesting that human Aurora-B is a mitotic histone H3 kinase.[1]

References

  1. Aurora-B associated protein phosphatases as negative regulators of kinase activation. Sugiyama, K., Sugiura, K., Hara, T., Sugimoto, K., Shima, H., Honda, K., Furukawa, K., Yamashita, S., Urano, T. Oncogene (2002) [Pubmed]
 
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