PASK (proline-alanine-rich Ste20-related kinase) binds to tubulin and microtubules and is involved in microtubule stabilization

Tomonari Tsutsumi, Takamitsu Kosaka, Hiroshi Ushiro, Kazushi Kimura, Tomoyuki Honda, Tetsuro Kayahara, Akira Mizoguchi

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


Proline-alanine-rich Ste20-related kinase (PASK, also referred to as SPAK) has been linked to ion transport regulation. Here, we report two novel activities of PASK: binding to tubulin and microtubules and the promotion of microtubule assembly. Tubulin binding assay showed that full-length PASK and its kinase domain bound to purified tubulin whereas the N-terminal or C-terminal non-catalytic domains of PASK did not. The full-length PASK and its kinase domain were sedimented with paclitaxel-stabilized microtubules by ultracentrifugation. These results indicate that the kinase domain of PASK can interact directly with both microtubules and soluble tubulin in vitro. Truncated PASK lacking the N-terminal non-catalytic domain promoted microtubule assembly at a subcritical concentration of purified tubulin. FLAG-PASK expressed in COS-7 cells translocated to the cytoskeleton when the cells were stimulated with hypertonic sodium chloride, and stabilized microtubules against depolymerization by nocodazole. Our findings suggest that PASK may regulate the cytoskeleton by modulating microtubule stability.

Original languageEnglish
Pages (from-to)267-278
Number of pages12
JournalArchives of Biochemistry and Biophysics
Issue number2
Publication statusPublished - Sept 15 2008
Externally publishedYes


  • Hyperosmotic stress
  • Microtubule
  • Microtubule-associated protein
  • Proline-alanine-rich Ste20-related kinase (PASK)
  • Protein kinase
  • Ste20-related proline-alanine-rich kinase (SPAK)

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology


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