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Kinesin-13s are microtubule (MT) depolymerases different from most other kinesins that move along MTs. Like other kinesins, they have a motor or head domain (HD) containing a tubulin and an ATP binding site. Interestingly, kinesin-13s have an additional binding site (Kin-Tub-2) on the opposite side of the HD that contains several family conserved positively charged residues. The role of this site in kinesin-13 function is not clear. To address this issue, we investigated the  in-vitro  and  in-vivo  effects of mutating Kin-Tub-2 family conserved residues on the   Drosophila melanogaster   kinesin-13, KLP10A. We show that the Kin-Tub-2 site enhances tubulin cross-linking and MT bundling properties of KLP10A  in-vitro . Disruption of the Kin-Tub-2 site, despite not having a deleterious effect on MT depolymerization, results in abnormal mitotic spindles and lagging chromosomes during mitosis in    Drosophila    S2 cells. The results suggest that the additional Kin-Tub-2 tubulin biding site plays a direct MT attachment role  in-vivo .

A Second Tubulin Binding Site on the Kinesin-13 Motor Head Domain Is Important during Mitosis