@article {1170241,
	title = {A Tubulin Binding Switch Underlies Kip3/Kinesin-8 Depolymerase Activity},
	journal = {Dev Cell},
	volume = {42},
	number = {1},
	year = {2017},
	month = {2017 07 10},
	pages = {37-51.e8},
	abstract = {Kinesin-8 motors regulate the size of microtubule structures, using length-dependent accumulation at the plus end to preferentially disassemble long microtubules. Despite extensive study, the kinesin-8 depolymerase mechanism remains under debate. Here, we provide evidence for an alternative, tubulin curvature-sensing model of microtubule depolymerization by the budding yeast kinesin-8, Kip3. Kinesin-8/Kip3 uses ATP hydrolysis, like other kinesins, for stepping on the microtubule lattice, but at the plus end Kip3 undergoes a switch: its ATPase activity is~suppressed when it binds tightly to the curved conformation of tubulin. This prolongs plus-end binding, stabilizes protofilament curvature, and ultimately promotes microtubule disassembly. The tubulin curvature-sensing model is supported by our identification of Kip3 structural elements necessary and sufficient for plus-end binding and depolymerase activity, as well as by the identification of an α-tubulin residue specifically required for the Kip3-curved tubulin interaction. Together, these findings elucidate a major regulatory mechanism controlling the size of cellular microtubule structures.},
	keywords = {Adenosine Triphosphate, Animals, Biocatalysis, Hydrolysis, Kinesin, Microtubules, Models, Biological, Models, Molecular, Mutant Proteins, Polymerization, Protein Binding, Protein Structure, Secondary, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sus scrofa, Tubulin},
	issn = {1878-1551},
	doi = {10.1016/j.devcel.2017.06.011},
	author = {Arellano-Santoyo, Hugo and Geyer, Elisabeth A and Stokasimov, Ema and Chen, Geng-Yuan and Su, Xiaolei and Hancock, William and Rice, Luke M and Pellman, David}
}
