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XB-ART-59832
Elife 2023 May 25;12. doi: 10.7554/eLife.85328.
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The structural basis of the multi-step allosteric activation of Aurora B kinase.

Segura-Peña D , Hovet O , Gogoi H , Dawicki-McKenna J , Hansen Wøien SM , Carrer M , Black BE , Cascella M , Sekulic N .


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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.

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Genes referenced: incenp

References [+] :
Abdul Azeez, Structural mechanism of synergistic activation of Aurora kinase B/C by phosphorylated INCENP. 2019, Pubmed