Abstract
Human Aurora/Ipl1-related kinase 2 (Aurora-B) is a key regulator of mitosis. Here human proteasome alpha-subunit C8 (HC8) was identified to interact with the Aurora-B by yeast two-hybrid screen. This finding was confirmed by GST pull-down assays and immunoprecipitation experiments. The Aurora-B protein level increased in HeLa cells cultured with proteasome inhibitor ALLN. Our data suggest that Aurora-B might undergo degradation by binding to HC8 in a proteasome-dependent manner during mitosis.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Aurora Kinase B
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Aurora Kinases
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Cell Cycle
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Cysteine Endopeptidases / chemistry*
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Cysteine Endopeptidases / metabolism*
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DNA, Complementary / metabolism
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Electrophoresis, Polyacrylamide Gel
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Glutathione Transferase / metabolism
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HeLa Cells
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Humans
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Immunoblotting
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Mitosis
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Multienzyme Complexes / metabolism*
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Plasmids / metabolism
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Precipitin Tests
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Proteasome Endopeptidase Complex
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Protein Binding
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Protein Biosynthesis
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Protein Serine-Threonine Kinases / chemistry
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Protein Serine-Threonine Kinases / metabolism*
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Two-Hybrid System Techniques
Substances
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DNA, Complementary
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Multienzyme Complexes
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Glutathione Transferase
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AURKB protein, human
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Aurora Kinase B
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Aurora Kinases
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Protein Serine-Threonine Kinases
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Cysteine Endopeptidases
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PSMA3 protein, human
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Proteasome Endopeptidase Complex