14-3-3 Proteins directly regulate Ca2+/calmodulin-dependent protein kinase kinase α through phosphorylation-dependent multisite binding

Tohru Ichimura, Masato Taoka, Yasukazu Hozumi, Kaoru Goto, Hiroshi Tokumitsu

Research output: Contribution to journalArticlepeer-review

18 Citations (Scopus)


Ca2+/calmodulin-dependent protein kinase kinase α (CaMKKα) plays critical roles in the modulation of neuronal cell survival as well as many other cellular activities. Here we show that 14-3-3 proteins directly regulate CaMKKα when the enzyme is phosphorylated by protein kinase A on either Ser74 or Ser475. Mutational analysis revealed that these two serines are both functional: the CaMKKα mutant with a mutation at either of these residues, but not the double mutant, was inhibited significantly by 14-3-3. The mode of regulation described herein differs the recently described mode of 14-3-3 regulation of CaMKKα.

Original languageEnglish
Pages (from-to)661-665
Number of pages5
JournalFEBS Letters
Issue number5
Publication statusPublished - Mar 5 2008
Externally publishedYes


  • 14-3-3 Protein
  • Calmodulin
  • Protein kinase
  • Proteomics
  • Signal transduction
  • cAMP

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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