Cell division ends when two daughter cells physically separate via abscission, the cleavage of the intercellular bridge. It is currently less clear how the anti-parallel microtubule bundles bridging daughter cells are severed. Here, we provide evidence for a novel abscission mechanism. We found that the chromokinesin KIF4A accumulates adjacent to the midbody during cytokinesis and is required for efficient abscission. KIF4A interacts with the microtubule destabilizer STMN1 as identified by mass spectrometry, providing mechanistic insight. This interaction is enhanced by SUMOylation of KIF4A. We mapped lysine 460 in KIF4A as SUMO acceptor site and employed CRISPR-Cas9 mediated genome editing to block SUMO conjugation of endogenous KIF4A, resulting in a delay in cytokinesis. Combined, our work provides novel insight in abscission regulation by a KIF4A, STMN1 and SUMO triad.