Source:http://linkedlifedata.com/resource/pubmed/id/21531210
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2011-5-23
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pubmed:abstractText |
Aurora-C, a member of the Aurora kinase family, is implicated in the regulation of mitosis. In contrast to Aurora-A and Aurora-B its cellular localization and functions are poorly characterized. TACC1 protein belongs to the transforming acidic coiled-coil family shown to interact with the Aurora kinases. In the present study we analyzed the interaction between Aurora-C and TACC1 by means of immunofluorescence (IF), co-immunoprecipitation (IP) and in vitro phosphorylation experiments. We demonstrated that Aurora-C and TACC1 proteins co-localize to the midbody of HeLa cells during cytokinesis. Immunoprecipitated TACC1 from HeLa cell extracts was associated with Aurora-C. In addition, the interaction of the two proteins was tested by analyzing the phosphorylation of TACC1 in vitro. The results demonstrated that TACC1 is phosphorylated by Aurora-C on a serine at position 228. In conclusion, the study demonstrated that TACC1 localizes at the midbody during cytokinesis and interacts with and is a substrate of Aurora-C, which warrant further investigation in order to elucidate the functional significance of this interaction.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Fetal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Microtubule-Associated Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/TACC1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/aurora kinase
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1090-2104
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pubmed:author |
pubmed-author:Arlot-BonnemainsYannickY,
pubmed-author:BaldiniEnkeE,
pubmed-author:CoccaroCarmelaC,
pubmed-author:CremetJean-YvesJY,
pubmed-author:D'ArmientoMassiminoM,
pubmed-author:GabillardJean-CharlesJC,
pubmed-author:PrigentClaudeC,
pubmed-author:SorrentiSalvatoreS,
pubmed-author:UlisseSalvatoreS
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pubmed:copyrightInfo |
Copyright © 2011 Elsevier Inc. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
20
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pubmed:volume |
408
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
647-53
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pubmed:meshHeading |
pubmed-meshheading:21531210-Cytokinesis,
pubmed-meshheading:21531210-Fetal Proteins,
pubmed-meshheading:21531210-HeLa Cells,
pubmed-meshheading:21531210-Humans,
pubmed-meshheading:21531210-Immunoprecipitation,
pubmed-meshheading:21531210-Microtubule-Associated Proteins,
pubmed-meshheading:21531210-Nuclear Proteins,
pubmed-meshheading:21531210-Phosphorylation,
pubmed-meshheading:21531210-Protein-Serine-Threonine Kinases,
pubmed-meshheading:21531210-Serine
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pubmed:year |
2011
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pubmed:articleTitle |
Aurora-C interacts with and phosphorylates the transforming acidic coiled-coil 1 protein.
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pubmed:affiliation |
CNRS-UMR 6061, Institut Génétique et Développement, IFR 140, UEB-Université Rennes 1, 2 Avenue du Pr Léon Bernard, Rennes Cedex, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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