CNRS-UMR 6061, Institut Génétique et Développement, IFR 140, UEB-Université Rennes 1, 2 Avenue du Pr Léon Bernard, Rennes Cedex, France.
Biochem Biophys Res Commun. 2011 May 20;408(4):647-53. doi: 10.1016/j.bbrc.2011.04.078. Epub 2011 Apr 21.
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.
极光激酶家族的一员 Aurora-C 参与有丝分裂的调控。与 Aurora-A 和 Aurora-B 不同，其细胞定位和功能尚未得到充分描述。TACC1 蛋白属于转化酸性卷曲螺旋家族，已知其与 Aurora 激酶相互作用。在本研究中，我们通过免疫荧光（IF）、共免疫沉淀（IP）和体外磷酸化实验分析了 Aurora-C 和 TACC1 之间的相互作用。我们证明 Aurora-C 和 TACC1 蛋白在 HeLa 细胞的胞质分裂过程中共同定位于中间体。从 HeLa 细胞提取物中免疫沉淀的 TACC1 与 Aurora-C 相关联。此外，通过分析体外 TACC1 的磷酸化来测试这两种蛋白质的相互作用。结果表明，TACC1 在丝氨酸 228 位被 Aurora-C 磷酸化。总之，该研究表明 TACC1 在胞质分裂过程中定位于中间体，并与 Aurora-C 相互作用并成为其底物，这值得进一步研究，以阐明这种相互作用的功能意义。
