Kinesin-14

Kinesin-14 motor proteins are ATP-dependent microtubule-based motors that move toward microtubule minus-ends, generating forces critical for mitotic spindle organization^[1][2]. Mechanistically, Kinesin-14s align antiparallel microtubules, crosslink spindle fibers, and regulate metaphase spindle length by balancing plus-end-directed motor forces^[3][4]. In fission yeast and human cells, Kinesin-14 interacts with the γ-tubulin ring complex (γ-TuRC) to modulate microtubule nucleation and spindle pole integrity^[5][6]. Loss of Kinesin-14 function can induce aneuploidy through kinesin-5-dependent microtubule protrusions that disrupt chromosome segregation during cytokinesis^[7]. Compared with related isoforms, such as Kinesin-5 or Kinesin-14 subtypes Ncd and HSET, Kinesin-14 exhibits unique tail and stalk domain interactions that determine minus-end-directed motility, crosslinking specificity, and spindle localization^[8][9][10]. Plant-specific Kinesin-14s, including OsKCH2, show inherent minus-end-directed processivity and can transport actin filaments along microtubules, compensating for the absence of cytoplasmic dynein^[11][2]. These properties make Kinesin-14 a target for experimental manipulation using small molecules or genetic perturbations to investigate spindle dynamics, microtubule organization, and chromosome segregation fidelity^[5][3].