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Journal Article

Stu2p, the budding yeast member of the conserved Dis1/XMAP215 family of microtubule-associated proteins is a plus end-binding microtubule destabilizer.

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van Breugel,  Mark
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Drechsel,  David
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Hyman,  Anthony
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Citation

van Breugel, M., Drechsel, D., & Hyman, A. (2003). Stu2p, the budding yeast member of the conserved Dis1/XMAP215 family of microtubule-associated proteins is a plus end-binding microtubule destabilizer. Journal of Cell Biology, 161(2), 359-369.


Cite as: https://hdl.handle.net/21.11116/0000-0001-12FC-F
Abstract
The Dis1/XMAP215 family of microtubule-associated proteins conserved from yeast to mammals is essential for cell division. XMAP215, the Xenopus member of this family, has been shown to stabilize microtubules in vitro, but other members of this family have not been biochemically characterized. Here we investigate the properties of the Saccharomyces cerevisiae homologue Stu2p in vitro. Surprisingly, Stu2p is a microtubule destabilizer that binds preferentially to microtubule plus ends. Quantitative analysis of microtubule dynamics suggests that Stu2p induces microtubule catastrophes by sterically interfering with tubulin addition to microtubule ends. These results reveal both a new biochemical activity for a Dis1/XMAP215 family member and a novel mechanism for microtubule destabilization.