biostudies-literatureCuijpers SAGEuropean Research CouncilEuropean UnionDutch Research Council (NWO)Wellcome TrustKWF KankerbestrijdingMarie Curie Actionjcs248591https://www.ebi.ac.uk/biostudies/studies/S-EPMC7390632biostudies-literatureUnknown133(14)Cell division ends when two daughter cells physically separate via abscission, the cleavage of the intercellular bridge. It is not clear how the anti-parallel microtubule bundles bridging daughter cells are severed. Here, we present a novel abscission mechanism. We identified chromokinesin KIF4A, which is adjacent to the midbody during cytokinesis, as being required for efficient abscission. KIF4A is regulated by post-translational modifications. We evaluated modification of KIF4A by the ubiquitin-like protein SUMO. We mapped lysine 460 in KIF4A as the SUMO acceptor site and employed CRISPR-Cas9-mediated genome editing to block SUMO conjugation of endogenous KIF4A. Failure to SUMOylate this site in KIF4A delayed cytokinesis. SUMOylation of KIF4A enhanced the affinity for the microtubule deJournal of cell scienceChromokinesin KIF4A teams up with stathmin 1 to regulate abscission in a SUMO-dependent manner.PMC739063210835107022/Z/15/Z107022607722310913724.016.003Vertegaal ACORuppert JGCuijpers SAGEarnshaw WCWillemstein Evan Elsland DMfalseChromokinesin KIF4A teams up with stathmin 1 to regulate abscission in a SUMO-dependent manner.Cell division ends when two daughter cells physically separate via abscission, the cleavage of the intercellular bridge. It is not clear how the anti-parallel microtubule bundles bridging daughter cells are severed. Here, we present a novel abscission mechanism. We identified chromokinesin KIF4A, which is adjacent to the midbody during cytokinesis, as being required for efficient abscission. KIF4A is regulated by post-translational modifications. We evaluated modification of KIF4A by the ubiquitin-like protein SUMO. We mapped lysine 460 in KIF4A as the SUMO acceptor site and employed CRISPR-Cas9-mediated genome editing to block SUMO conjugation of endogenous KIF4A. Failure to SUMOylate this site in KIF4A delayed cytokinesis. SUMOylation of KIF4A enhanced the affinity for the microtubule de2020-01-01T00:00:00Z2020 Jul2026-05-04T23:42:24.744Z2021-02-20T09:39:56ZS-EPMC73906323259148110.1242/jcs.248591