Kinesin-13

Kinesin-13 proteins are specialized microtubule (MT) depolymerases that regulate MT length by promoting tubulin removal at both ends^[1][2]. Unlike conventional motile kinesins, Kinesin-13 motors form ring and spiral oligomers at MT ends, which stabilizes their position for efficient depolymerization^[1][3]. Mechanistically, the conserved neck and loop-2 regions of Kinesin-13 coordinate ATP turnover to induce tubulin curvature and facilitate protofilament disassembly^[3][4][5]. This depolymerization is critical for spindle assembly, kinetochore-MT attachment, and accurate chromosome segregation during mitosis and meiosis^[2][6][7]. In disease models, Kinesin-13 dysregulation alters spindle morphology and microtubule flux, influencing cell division fidelity and axon regeneration^[8][9][10]. Compared with related isoforms such as Kinesin-8, Kinesin-13 exhibits higher end-specific depolymerization activity and distinct structural elements, including the α4-helix and KVD motif, which are essential for MT-end recognition^[11][12][13]. Kinesin-13 inhibitors and mutants that disrupt neck-mediated depolymerization or ATPase activity allow precise experimental modulation of MT dynamics for cell division and neuronal studies^[6][7]. Collectively, the Kinesin-13 family serves as a versatile model for understanding controlled MT depolymerization, isoform-specific regulation, and targeted cytoskeletal interventions in diverse eukaryotic systems^[14][15].