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

doi:10.1083/jcb.200211097

Published 28 April 2003. doi:10.1083/jcb.200211097

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© The Rockefeller University Press, 0021-9525/2003/4/359 $5.00
The Journal of Cell Biology, Volume 161, Number 2, 359-369

Article

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

Mark van Breugel, David Drechsel and Anthony Hyman

Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany

Address correspondence to Anthony Hyman, Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01307 Dresden, Germany. Tel.: 49-351-210-1280. Fax: 49-351-210-1289. E-mail: hyman{at}mpi-cbg.de

The Dis1/XMAP215 family of microtubule-associated proteins conservedfrom yeast to mammals is essential for cell division. XMAP215,the Xenopus member of this family, has been shown to stabilizemicrotubules in vitro, but other members of this family havenot been biochemically characterized. Here we investigate theproperties of the Saccharomyces cerevisiae homologue Stu2p invitro. Surprisingly, Stu2p is a microtubule destabilizer thatbinds preferentially to microtubule plus ends. Quantitativeanalysis of microtubule dynamics suggests that Stu2p inducesmicrotubule catastrophes by sterically interfering with tubulinaddition to microtubule ends. These results reveal both a newbiochemical activity for a Dis1/XMAP215 family member and anovel mechanism for microtubule destabilization.

Key Words: microtubule; dynamics; assembly; XMAP215; Dis1

The online version of this article includes supplemental material.

^* Abbreviations used in this paper: HU, hydroxyurea; VE-DIC, video-enhanceddifferential interference contrast microscopy.

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