Suppression of death-associated protein kinase 2 by interaction with 14-3-3 proteins

被引：21

作者：

Yuasa, Keizo ^{[1
]}

Ota, Reina ^{[1
]}

Matsuda, Shinya ^{[1
]}

Isshiki, Kinuka ^{[1
]}

Inoue, Masahiro ^{[2
]}

Tsuji, Akihiko ^{[1
]}

机构：

[1] Univ Tokushima, Grad Sch, Dept Biol Sci & Technol, Tokushima 770, Japan

[2] Kurume Univ, Sch Med, Dept Infect Med, Div Eukaryot Microbiol, Kurume, Fukuoka 830, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2015年 / 464卷 / 01期

关键词：

DAPK2; Apoptosis; 14-3-3; Akt; STRUCTURAL BASIS; CELL-DEATH; APOPTOSIS; PHOSPHORYLATION; DAPK; BAD; DEPHOSPHORYLATION; ACTIVATION; BINDING; FAMILY;

D O I：

10.1016/j.bbrc.2015.05.105

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Death-associated protein kinase 2 (DAPK2), a Ca2+/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. (C) 2015 Elsevier Inc. All rights reserved.

引用

页码：70 / 75

页数：6

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