AI Article Synopsis
- Kinesin-13s are unique microtubule depolymerases with a motor head domain and an additional binding site called Kin-Tub-2, whose function remains unclear.
- Research on KLP10A in Drosophila shows that the Kin-Tub-2 site enhances its ability to cross-link tubulin and bundle microtubules in vitro.
- Mutating the Kin-Tub-2 site disrupts normal mitotic spindle formation and leads to issues like lagging chromosomes during cell division, indicating its important role in microtubule attachment in vivo.
Article Abstract
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.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3755979 | PMC |
| http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0073075 | PLOS |
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