RT Journal Article SR Electronic T1 Spatiotemporal organization of Aurora-B by APC/CCdh1 after mitosis coordinates cell spreading through FHOD1 JF Journal of Cell Science JO J. Cell Sci. FD The Company of Biologists Ltd SP 2845 OP 2856 DO 10.1242/jcs.123232 VO 126 IS 13 A1 Floyd, Suzanne A1 Whiffin, Nicola A1 Gavilan, Maria P. A1 Kutscheidt, Stefan A1 De Luca, Maria A1 Marcozzi, Chiara A1 Min, Mingwei A1 Watkins, Johnathan A1 Chung, Kathryn A1 Fackler, Oliver T. A1 Lindon, Catherine YR 2013 UL http://jcs.biologists.org/content/126/13/2845.abstract AB Spatiotemporal regulation of mitotic kinase activity underlies the extensive rearrangement of cellular components required for cell division. One highly dynamic mitotic kinase is Aurora-B (AurB), which has multiple roles defined by the changing localisation of the chromosome passenger complex (CPC) as cells progress through mitosis, including regulation of cytokinesis and abscission. Like other mitotic kinases, AurB is a target of the anaphase-promoting complex (APC/C) ubiquitin ligase during mitotic exit, but it is not known if APC/C-mediated destruction plays any specific role in controlling AurB activity. We have examined the contribution of the Cdh1 coactivator-associated APC/CCdh1 to the organization of AurB activity as cells exit mitosis and re-enter interphase. We report that APC/CCdh1-dependent proteolysis restricts a cell-cortex-associated pool of active AurB in space and time. In early G1 phase this pool of AurB is found at protrusions associated with cell spreading. AurB retention at the cortex depends on a formin, FHOD1, critically required to organize the cytoskeleton after division. We identify AurB phosphorylation sites in FHOD1 and show that phosphomutant FHOD1 is impaired in post-mitotic assembly of oriented actin cables. We propose that Cdh1 contributes to spatiotemporal organization of AurB activity and that organization of FHOD1 activity by AurB contributes to daughter cell spreading after mitosis.