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 journalArticle

14 Citations (Scopus)

Abstract

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
Volume582
Issue number5
DOIs
Publication statusPublished - Mar 5 2008
Externally publishedYes

Fingerprint

14-3-3 Proteins
Calcium-Calmodulin-Dependent Protein Kinases
Phosphorylation
Phosphotransferases
Cyclic AMP-Dependent Protein Kinases
Serine
Cell Survival
Cells
Modulation
Mutation
Enzymes

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

14-3-3 Proteins directly regulate Ca2+/calmodulin-dependent protein kinase kinase α through phosphorylation-dependent multisite binding. / Ichimura, Tohru; Taoka, Masato; Hozumi, Yasukazu; Goto, Kaoru; Tokumitsu, Hiroshi.

In: FEBS Letters, Vol. 582, No. 5, 05.03.2008, p. 661-665.

Research output: Contribution to journalArticle

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