A TOGL domain specifically targets yeast CLASP to kinetochores to stabilize kinetochore microtubules

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Caroline Funk1, Verena Schmeiser1, Jennifer Ortiz1

  • 1Biochemie-Zentrum der Universität Heidelberg, 69120 Heidelberg, Germany.

The Journal of Cell Biology
|May 28, 2014
PubMed

Insights

The two TOG-like domains of yeast CLASP Stu1 have distinct roles in cell division. TOGL2 binds tubulin for spindle microtubule polymerization, while TOGL1 stabilizes kinetochore microtubules.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Cytoplasmic linker-associated proteins (CLASPs) are crucial for cell division.
  • CLASPs possess multiple TOG-like (TOGL) domains, implicated in tubulin binding.
  • The specific functions of individual TOGL domains within CLASPs are not fully elucidated.

Purpose of the Study:

  • To investigate the distinct roles of the two TOGL domains in Saccharomyces cerevisiae CLASP Stu1 during cell division.
  • To determine how Stu1 is localized to microtubules during different mitotic phases.
  • To elucidate the specific functions of Stu1's TOGL domains in microtubule dynamics and kinetochore-microtubule attachments.

Main Methods:

  • Yeast genetics and live-cell imaging.
  • Tubulin binding assays.
  • Analysis of microtubule polymerization and stability in vivo.

Main Results:

  • Only the TOGL2 domain of Stu1 directly binds tubulin and is essential for spindle microtubule polymerization.
  • The TOGL1 domain recruits Stu1 to kinetochores, ensuring kinetochore microtubule stability and tension.
  • Stu1 exhibits distinct localization patterns to spindle microtubules during metaphase and anaphase, with TOGL2 activity crucial for interpolar microtubule stability.

Conclusions:

  • The two TOGL domains of yeast CLASP Stu1 possess divergent functions.
  • TOGL2 is primarily involved in microtubule polymerization and interpolar spindle stability.
  • TOGL1 plays a critical role in kinetochore-microtubule regulation and stability.

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