Suppression of death-associated protein kinase 2 by interaction with 14-3-3 proteins
Copyright policy )Suppression of death-associated protein kinase 2 by interaction with 14-3-3 proteins
Death-associated protein kinase 2 (DAPK2), a Ca(2+)/calmodulin-regulated serine/threonine kinase, induces apoptosis. However, the signaling mechanisms involved in this process are unknown. Using a proteomic approach, we identified 14-3-3 proteins as novel DAPK2-interacting proteins. The 14-3-3 family has the ability to bind to phosphorylated proteins via recognition of three conserved amino acid motifs (mode 1-3 motifs), and DAPK2 contains the mode 3 motif ((pS/pT)X1-2-COOH). The interaction of 14-3-3 proteins with DAPK2 was dependent on the phosphorylation of Thr(369), and effectively suppressed DAPK2 kinase activity and DAPK2-induced apoptosis. Furthermore, we revealed that the 14-3-3 binding site Thr(369) of DAPK2 was phosphorylated by the survival kinase Akt. Our findings suggest that DAPK2-induced apoptosis is negatively regulated by Akt and 14-3-3 proteins.
- University of Tokushima Japan
- Kurume University Japan
Binding Sites, Calcineurin, Amino Acid Motifs, Molecular Sequence Data, Apoptosis, Death-Associated Protein Kinases, 14-3-3 Proteins, Gene Expression Regulation, COS Cells, Chlorocebus aethiops, Exoribonucleases, Biomarkers, Tumor, MCF-7 Cells, Animals, Humans, Phosphorylation, Proto-Oncogene Proteins c-akt, Plasmids, Protein Binding, Signal Transduction
Binding Sites, Calcineurin, Amino Acid Motifs, Molecular Sequence Data, Apoptosis, Death-Associated Protein Kinases, 14-3-3 Proteins, Gene Expression Regulation, COS Cells, Chlorocebus aethiops, Exoribonucleases, Biomarkers, Tumor, MCF-7 Cells, Animals, Humans, Phosphorylation, Proto-Oncogene Proteins c-akt, Plasmids, Protein Binding, Signal Transduction
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