{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Cuijpers SAG"],"funding":["European Research Council","European Union","Dutch Research Council (NWO)","Wellcome Trust","KWF Kankerbestrijding","Marie Curie Action"],"pagination":["jcs248591"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7390632"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["133(14)"],"pubmed_abstract":["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 de"],"journal":["Journal of cell science"],"pubmed_title":["Chromokinesin KIF4A teams up with stathmin 1 to regulate abscission in a SUMO-dependent manner."],"pmcid":["PMC7390632"],"funding_grant_id":["10835","107022/Z/15/Z","107022","607722","310913","724.016.003"],"pubmed_authors":["Vertegaal ACO","Ruppert JG","Cuijpers SAG","Earnshaw WC","Willemstein E","van Elsland DM"],"additional_accession":[]},"is_claimable":false,"name":"Chromokinesin KIF4A teams up with stathmin 1 to regulate abscission in a SUMO-dependent manner.","description":"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 de","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Jul","modification":"2026-05-04T23:42:24.744Z","creation":"2021-02-20T09:39:56Z"},"accession":"S-EPMC7390632","cross_references":{"pubmed":["32591481"],"doi":["10.1242/jcs.248591"]}}