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| == Function == | | == Function == |
| [https://www.uniprot.org/uniprot/KI10A_DROME KI10A_DROME] Required during anaphase to drive sister chromatid separation to promote flux by actively depolymerizing kinetochore microtubules at their pole-associated minus ends, thereby moving chromatids through a "poleward flux".<ref>PMID:14681690</ref> | | [https://www.uniprot.org/uniprot/KI10A_DROME KI10A_DROME] Required during anaphase to drive sister chromatid separation to promote flux by actively depolymerizing kinetochore microtubules at their pole-associated minus ends, thereby moving chromatids through a "poleward flux".<ref>PMID:14681690</ref> |
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| == Publication Abstract from PubMed ==
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| To elucidate the structural basis of the mechanism of microtubule depolymerization by kinesin-13s, we analyzed complexes of tubulin and the Drosophila melanogaster kinesin-13 KLP10A by electron microscopy (EM) and fluorescence polarization microscopy. We report a nanometer-resolution (1.1 nm) cryo-EM three-dimensional structure of the KLP10A head domain (KLP10AHD) bound to curved tubulin. We found that binding of KLP10AHD induces a distinct tubulin configuration with displacement (shear) between tubulin subunits in addition to curvature. In this configuration, the kinesin-binding site differs from that in straight tubulin, providing an explanation for the distinct interaction modes of kinesin-13s with the microtubule lattice or its ends. The KLP10AHD-tubulin interface comprises three areas of interaction, suggesting a crossbow-type tubulin-bending mechanism. These areas include the kinesin-13 family conserved KVD residues, and as predicted from the crossbow model, mutating these residues changes the orientation and mobility of KLP10AHDs interacting with the microtubule.
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| Structural Model for Tubulin Recognition and Deformation by Kinesin-13 Microtubule Depolymerases.,Asenjo AB, Chatterjee C, Tan D, Depaoli V, Rice WJ, Diaz-Avalos R, Silvestry M, Sosa H Cell Rep. 2013 Feb 19. pii: S2211-1247(13)00054-5. doi:, 10.1016/j.celrep.2013.01.030. PMID:23434508<ref>PMID:23434508</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| ==See Also== | | ==See Also== |