Polo kinase mediates the phosphorylation and cellular localization of Nuf/FIP3, a Rab11 effector.

Animal cytokinesis involves both actin-myosin-based contraction and vesicle-mediated membrane addition. In many cell types, including early Drosophila embryos, Nuf/FIP3, a Rab11 effector, mediates recycling endosome (RE)-based vesicle delivery to the cytokinesis furrow. Nuf exhibits a cell cycle-regulated concentration at the centrosome that is accompanied by dramatic changes in its phosphorylation state. Here we demonstrate that maximal phosphorylation of Nuf occurs at prophase, when centrosome-associated Nuf disperses throughout the cytoplasm. Accordingly, ectopic Cdk1 activation results in immediate Nuf dispersal from the centrosome. Screening of candidate kinases reveals a specific, dosage-sensitive interaction between Nuf and Polo with respect to Nuf-mediated furrow formation. Inhibiting Polo activity results in Nuf underphosphorylation and prolonged centrosome association. In vitro, Polo directly binds and is required for Nuf phosphorylation at Ser-225 and Thr-227, matching previous in vivo-mapped phosphorylation sites. These results demonstrate a role for Polo kinase in directly mediating Nuf cell cycle-dependent localization. © 2017 Brose, Crest, et al. This article is distributed by The American Society for under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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