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

作者：Gabillard Jean Charles; Ulisse Salvatore; Baldini Enke; Sorrenti Salvatore; Cremet Jean Yves; Coccaro Carmela; Prigent Claude; D'Armiento Massimino; Arlot Bonnemains Yannick^*

来源：Biochemical and Biophysical Research Communications, 2011, 408(4): 647-653.

DOI：10.1016/j.bbrc.2011.04.078

• Aurora-C
• Kinase
• TACC1
• Midbody
• Cytokinesis

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 TACO 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.

• 出版日期2011-5-20