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Aurora-C interacts with and phosphorylates the transforming acidic coiled-coil 1 protein.

Abstract : 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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Contributor : Hervé De Villemeur Connect in order to contact the contributor
Submitted on : Monday, May 9, 2011 - 10:52:04 AM
Last modification on : Wednesday, March 30, 2022 - 2:35:23 PM



Jean-Charles Gabillard, Salvatore Ulisse, Enke Baldini, Salvatore Sorrenti, Jean-Yves Cremet, et al.. Aurora-C interacts with and phosphorylates the transforming acidic coiled-coil 1 protein.. Biochemical and Biophysical Research Communications, Elsevier, 2011, 408 (4), pp.647-53. ⟨10.1016/j.bbrc.2011.04.078⟩. ⟨inserm-00591406⟩



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