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Publication Abstract from PubMed

Kinesin-13s are critical microtubule regulators which induce microtubule disassembly in an ATP dependent manner. To clarify their mechanism, we report here the crystal structure of a functional construct of the kinesin-13 Kif2C/MCAK in an ATP-like state and bound to the alphabeta-tubulin heterodimer, a complex mimicking the species that dissociates from microtubule ends during catalytic disassembly. Our results picture how Kif2C stabilizes a curved tubulin conformation. The Kif2C alpha4-L12-alpha5 region undergoes a remarkable 25 degrees rotation upon tubulin binding to target the alphabeta-tubulin hinge. This movement leads the beta5a-beta5b motif to interact with the distal end of beta-tubulin, whereas the neck and the KVD motif, two specific elements of kinesin-13s, target the alpha-tubulin distal end. Taken together with the study of Kif2C mutants, our data suggest that stabilization of a curved tubulin is an important contribution to the Kif2C mechanism.Kinesin-13s are microtubule depolymerizing enzymes. Here the authors present the crystal structure of a DARPin fused construct comprising the short neck region and motor domain of kinesin-13 in complex with an alphabeta-tubulin heterodimer, which shows that kinesin-13 functions by stabilizing a curved tubulin conformation.

Insight into microtubule disassembly by kinesin-13s from the structure of Kif2C bound to tubulin.,Wang W, Cantos-Fernandes S, Lv Y, Kuerban H, Ahmad S, Wang C, Gigant B Nat Commun. 2017 Jul 10;8(1):70. doi: 10.1038/s41467-017-00091-9. PMID:28694425^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.