Dephosphorylation of Microtubule‐Associated Protein 2, τ Factor, and Tubulin by Calcineurin

Satoshi Goto, Hideyuki Yamamoto, Kohji Fukunaga, Takafumi Iwasa, Yasuhiko Matsukado, Eishichi Miyamoto

Research output: Contribution to journalArticlepeer-review

150 Citations (Scopus)


Abstract: Calcineurin dephosphorylated microtubule‐associated protein 2 (MAP2) and τ factor phosphorylated by cyclic AMP‐dependent and Ca2+, calmodulin‐dependent protein kinases from the brain. Tubulin, only phosphorylated by the Ca2+, calmodulin‐dependent protein kinase, served as substrate for calcineurin. The concentrations of calmodulin required to give half‐maximal activation of calcineurin were 21 and 16 nM with MAP2 and τ factor as substrates, respectively. The Km and Vmaxvalues were in ranges of 1–3 μM and 0.4–1.7 μmol/mg/ min, respectively, for MAP2 and τ factor. The Km value for tubulin was in a similar range, but the Vmax value was lower. The peptide map analysis revealed that calcineurin dephosphorylated MAP2 and τ factor universally, but not in a site‐specific manner. The autophosphorylated Ca2+, calmodulin‐dependent protein kinase was not dephosphorylated by calcineurin. These results suggest that calcineurin plays an important role in the functions of microtubules via dephosphorylation.

Original languageEnglish
Pages (from-to)276-283
Number of pages8
JournalJournal of Neurochemistry
Issue number1
Publication statusPublished - 1985 Jan 1
Externally publishedYes


  • Ca, calmodulin‐dependent protein kinase
  • Calcineurin
  • Cyclic AMP‐dependent protein kinase
  • Microtubule‐associated protein 2
  • Tubulin
  • τ factor

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience


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