Aurora B, together with IN-box, the C-terminal part of INCENP, forms an enzymatic complex that ensures faithful cell division. The [Aurora B/IN-box] complex is activated by autophosphorylation in the Aurora B activation loop and in IN-box, but it is not clear how these phosphorylations activate the enzyme. We used a combination of experimental and computational studies to investigate the effects of phosphorylation on the molecular dynamics and structure of [Aurora B/IN-box]. In addition, we generated partially phosphorylated intermediates to analyze the contribution of each phosphorylation independently. We found that the dynamics of Aurora and IN-box are interconnected, and IN-box plays both positive and negative regulatory roles depending on the phosphorylation status of the enzyme complex. Phosphorylation in the activation loop of Aurora B occurs intramolecularly and prepares the enzyme complex for activation, but two phosphorylated sites are synergistically responsible for full enzyme activity.

中文翻译：

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极光B激酶多步变构激活的结构基础

Aurora B 与 INCENP 的 C 端部分 IN-box 一起形成酶促复合物，确保忠实的细胞分裂。[Aurora B/IN-box] 复合物由 Aurora B 激活环和 IN-box 中的自磷酸化激活，但尚不清楚这些磷酸化如何激活酶。我们结合实验和计算研究来研究磷酸化对 [Aurora B/IN-box] 的分子动力学和结构的影响。此外，我们生成了部分磷酸化的中间体来独立分析每个磷酸化的贡献。我们发现 Aurora 和 IN-box 的动力学是相互关联的，IN-box 根据酶复合物的磷酸化状态发挥正负调节作用。