Abstract
Aurora kinases are key regulators of cell division and important targets for cancer therapy. We report that Binucleine 2 is a highly isoform-specific inhibitor of Drosophila Aurora B kinase, and we identify a single residue within the kinase active site that confers specificity for Aurora B. Using Binucleine 2, we show that Aurora B kinase activity is not required during contractile ring ingression, providing insight into the mechanism of cytokinesis.
Publication types
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Letter
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Aurora Kinase B
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Aurora Kinases
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Cell Cycle Proteins / antagonists & inhibitors
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Cell Cycle Proteins / chemistry
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Cell Cycle Proteins / physiology*
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Cytokinesis / drug effects
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Cytokinesis / physiology*
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Drosophila Proteins / antagonists & inhibitors
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Drosophila Proteins / chemistry
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Drosophila Proteins / physiology*
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Drosophila melanogaster / cytology*
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Drosophila melanogaster / drug effects
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Drosophila melanogaster / enzymology*
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Isoenzymes / antagonists & inhibitors
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Isoleucine / chemistry
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Molecular Sequence Data
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Protein Kinase Inhibitors / chemistry
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Protein Kinase Inhibitors / pharmacology*
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Protein Serine-Threonine Kinases / antagonists & inhibitors
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Protein Serine-Threonine Kinases / chemistry
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Protein Serine-Threonine Kinases / physiology*
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Pyrazoles / chemistry*
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Pyrazoles / pharmacology
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RNA Interference
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Schiff Bases / chemistry*
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Schiff Bases / pharmacology
Substances
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Cell Cycle Proteins
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Drosophila Proteins
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Isoenzymes
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Protein Kinase Inhibitors
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Pyrazoles
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Schiff Bases
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binucleine 2
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Isoleucine
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AurB protein, Drosophila
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Aurora Kinase B
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Aurora Kinases
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Protein Serine-Threonine Kinases