Small Molecule Inhibitors of Aurora-A Induce Proteasomal Degradation of N-Myc in Childhood Neuroblastoma

(Cancer Cell 24, 75–89; July 8, 2013) In the original Figure 7C, the authors mistakenly used the same control histology panel twice: the top left and bottom left panels are identical. The authors regret this error and apologize for any confusion that it may have caused. This has now been corrected in the figure below. Small Molecule Inhibitors of Aurora-A Induce Proteasomal Degradation of N-Myc in Childhood NeuroblastomaBrockmann et al.Cancer CellJune 20, 2013In BriefAmplification of MYCN is a driver mutation in a subset of human neuroendocrine tumors, including neuroblastoma. No small molecules that target N-Myc, the protein encoded by MYCN, are clinically available. N-Myc forms a complex with the Aurora-A kinase, which protects N-Myc from proteasomal degradation. Although stabilization of N-Myc does not require the catalytic activity of Aurora-A, we show here that two Aurora-A inhibitors, MLN8054 and MLN8237, disrupt the Aurora-A/N-Myc complex and promote degradation of N-Myc mediated by the Fbxw7 ubiquitin ligase. Full-Text PDF Open Archive