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

Jawdat Al-Bassam, Mark Van Breugel, Stephen C. Harrison, Anthony Hyman

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Abstract

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 NH 2 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.

Original languageEnglish (US)
Pages (from-to)1009-1022
Number of pages14
JournalJournal of Cell Biology
Volume172
Issue number7
DOIs
StatePublished - Mar 2006
Externally publishedYes

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ASJC Scopus subject areas

  • Cell Biology

Cite this

Al-Bassam, J., Van Breugel, M., Harrison, S. C., & Hyman, A. (2006). Stu2p binds tubulin and undergoes an open-to-closed conformational change. Journal of Cell Biology, 172(7), 1009-1022. https://doi.org/10.1083/jcb.200511010