共 32 条
Covalent modification of human homeodomain interacting protein kinase 2 by SUMO-1 at lysine 25 affects its stability
被引:41
作者:

Gresko, E
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机构:
Univ Bern, Dept Chem & Biochem, CH-3012 Bern, Switzerland Univ Bern, Dept Chem & Biochem, CH-3012 Bern, Switzerland

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Roscic, A
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机构:
Univ Bern, Dept Chem & Biochem, CH-3012 Bern, Switzerland Univ Bern, Dept Chem & Biochem, CH-3012 Bern, Switzerland

Schmitz, ML
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机构:
Univ Bern, Dept Chem & Biochem, CH-3012 Bern, Switzerland Univ Bern, Dept Chem & Biochem, CH-3012 Bern, Switzerland
机构:
[1] Univ Bern, Dept Chem & Biochem, CH-3012 Bern, Switzerland
关键词:
HIPK2;
SUMO-1;
Ubc9;
p53;
D O I:
10.1016/j.bbrc.2005.02.113
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:
The HIPK2 protein is a critical regulator of apoptosis and functionally interacts with p53 to increase gene expression. Here we show that human HIPK2 is modified by sumoylation at lysine 25, as revealed by in vivo and in vitro experiments. While SUMO-1 modification of HIPK2 has no influence on its ability to phosphorylate p53 at serine 46, to induce gene expression, and to mediate apoptosis, a non-sumoylatable HIPK2 mutant displays a strongly increased protein stability. The N-terminal SUMO-1 modification site is conserved between all vertebrate HIPK2 proteins and is found in all members of the HIPK family of protein kinases. Accordingly, also human HIPK3 is modified by sumoylation. (c) 2005 Elsevier Inc. All rights reserved.
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页码:1293 / 1299
页数:7
相关论文
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