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Published 27 March 2006. doi:10.1083/jcb.200511010
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 172, Number 7, 1009-1022
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Article

 Stu2p binds tubulin and undergoes an open-to-closed conformational change

Jawdat Al-Bassam1, Mark van Breugel3, Stephen C. Harrison1,2, and Anthony Hyman3

1 Department of Biological Chemistry and Molecular Pharmacology and 2 Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115
3 Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany

Correspondence to Anthony Hyman: hyman{at}mpi-cbg.de

Stu2p from budding yeast belongs to the conserved Dis1/XMAP215 family of microtubule-associated proteins (MAPs). The common feature of proteins in this family is the presence of HEAT repeat–containing TOG domains near the NH2 terminus. We have investigated the functions of the two TOG domains of Stu2p in vivo and in vitro. Our data suggest that Stu2p regulates microtubule dynamics through two separate activities. First, Stu2p binds to a single free tubulin heterodimer through its first TOG domain. A large conformational transition in homodimeric Stu2p from an open structure to a closed one accompanies the capture of a single free tubulin heterodimer. Second, Stu2p has the capacity to associate directly with microtubule ends, at least in part, through its second TOG domain. These two properties lead to the stabilization of microtubules in vivo, perhaps by the loading of tubulin dimers at microtubule ends. We suggest that this mechanism of microtubule regulation is a conserved feature of the Dis1/XMAP215 family of MAPs.

J. Al-Bassam and M. van Breugel contributed equally to this paper.

M. van Breugel's present address is Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 2QH, United Kingdom.

Abbreviations used in this paper: MAP, microtubule-associated protein; MCAK, mitotic centromere-associated kinesin; NHS, N-hydroxysuccinimide; SPB, spindle pole body; TAP, tandem affinity purification.


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