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. 2015 Jun 9;5:10449. doi: 10.1038/srep10449

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Copyright © 2015, Macmillan Publishers Limited

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Kinase regulators Mob1 and Mob2 competitively bind NDR1. Mob1-bound NDR1 is active with phosphorylation on Ser281 and Thr444, while Mob2-bound NDR1 is inactive. In normal mitosis, PLK1 phosphorylates NDR1 on three sites (Thr7, Thr183 and Thr407), switching NDR1 from Mob1-binding to Mob2-binding, hence prevents NDR1 from Mob1-elicited activation to ensure proper spindle orientation. In the case of reversal PLK1-elicited suppression of NDR1, the cortical localization of LGN-NuMA is liberated which leads to aberrant mitotic spindle orientation.