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. 2021 May 13;40(23):3917–3928. doi: 10.1038/s41388-021-01766-w

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© The Author(s) 2021

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 2 — A Aurora-A can increase Myc expression directly, through promoter shift, in combination with hnRNP K; a potential indirect effect, also mediated by hnRNP K, may also represent an indirect Aurora-A contribution to elevated Myc levels. The right panel schematises the transcriptional effect of Aurora-A on FOXM1 gene expression. The dashed arrow indicates potential direct binding of an Aurora-A/FOXM1 complex to the FOXM1 promoter. In turn, Myc and FOXM1 can upregulate AURKA gene expression. B The N-Myc protein sequence is schematically represented on top; myc boxes and DNA-binding domains are indicated, as well as the binding regions to Aurora-A and FBXW7. FBXW7 recognises and ubiquitinates N-Myc, inducing proteasome-mediated degradation (lower left panel). Aurora-A binding protects N-Myc from FBXW7-mediated degradation (lower right panel). Created with BioRender.com.