KIF14 as a Dual Microtubule/F-Actin Binding Protein Contributing to Cytokinesis

Cytokinesis, the final step of cell division, necessitates precise coordination between the microtubule-based central spindle and the actomyosin contractile ring. KIF14, a member of the kinesin-3 family of motor proteins, has emerged as a crucial integrator of these cytoskeletal systems. This review consolidates recent advances in understanding KIF14's structural domains, its dual-binding capacity for microtubules and F-actin, and its mechanochemical characteristics. KIF14 collaborates with protein regulator of cytokinesis 1 (PRC1) to bundle and slide antiparallel microtubules, while phosphorylation mediated by NIMA related kinase 7 (Nek7) enables KIF14 to bind and transport Citron kinase (CIT-K) to the midbody. This process connects central spindle organization to RhoA-driven contractility. In addition, KIF14 interacts with centralspindlin components and actomyosin regulators, thereby reinforcing midzone integrity and promoting cleavage furrow ingression. Its persistent midbody localization and activity regulated by phosphorylation ensure the temporal coordination of late cytokinesis events. Collectively, these functions establish KIF14 as a dual-function integrator of spindle architecture and contractile-ring constriction, making it indispensable for successful cell division.