TY - DATA T1 - Video S1 from Coordinated regulation of the ESCRT-III component CHMP4C by the chromosomal passenger complex and centralspindlin during cytokinesis PY - 2016/10/18 AU - Luisa Capalbo AU - Ioanna Mela AU - Maria Alba Abad AU - A. Arockia Jeyaprakash AU - J. Michael Edwardson AU - Pier Paolo D'Avino UR - https://rs.figshare.com/articles/media/Video_S1_from_Coordinated_regulation_of_the_ESCRT-III_component_CHMP4C_by_the_chromosomal_passenger_complex_and_centralspindlin_during_cytokinesis/4038204 DO - 10.6084/m9.figshare.4038204.v1 L4 - https://ndownloader.figshare.com/files/6501438 KW - Aurora B KW - cell division KW - centralspindlin KW - cytokinesis KW - midbody KW - membrane remodelling N2 - The chromosomal passenger complex (CPC) - composed of Aurora B kinase, Borealin, Survivin and INCENP - surveys the fidelity of genome segregation throughout cell division. The CPC has been proposed to prevent polyploidy by controlling the final separation or abscission, of the two daughter cells via regulation of the ESCRT-III CHMP4C component. The molecular details are, however, still unclear. Using atomic force microscopy, we show that CHMP4C binds to and remodels membranes in vitro. Borealin prevents the association of CHMP4C with membranes, whereas Aurora B interferes with CHMP4C's membrane remodelling activity. Moreover, we show that CHMP4C phosphorylation is not required for its assembly into spiral filaments at the abscission site and that two distinctly localized pools of phosphorylated CHMP4C exist during cytokinesis. We also characterized the CHMP4C interactome in telophase cells and show that the centralspindlin complex associates preferentially with unphosphorylated CHMP4C in cytokinesis. Our findings indicate that gradual dephosphorylation of CHMP4C triggers a 'relay' mechanism between the CPC and centralspindlin that regulates the timely distribution and activation of CHMP4C for the execution of abscission. ER -