UV-light induces p38 MAPK-dependent phosphorylation of Bcl10

被引：28

作者：

Bodero, AJ

Ye, RQ

Lees-Miller, SP

机构：

[1] Univ Calgary, Dept Biochem & Mol Biol, Calgary, AB T2N 4N1, Canada

[2] Univ Calgary, Dept Biol Sci, Calgary, AB T2N 4N1, Canada

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2003年 / 301卷 / 04期

基金：

加拿大健康研究院;

关键词：

Bcl10; p38; stress-activated protein kinase; phosphorylation; UV; SB203580; PD169316;

D O I：

10.1016/S0006-291X(03)00063-9

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：

Bcl10 is a signaling protein required for activation of the NF-kappaB transcription factor. NF-kappaB is an important mediator of genotoxic stress and regulates the expression of genes required for both cell proliferation and cell death. Bcl10 is phosphorylated in vivo, however, the protein kinase or kinases responsible are not known. Here, we show that Bcl10 is phosphorylated in response to UV irradiation. UV-induced phosphorylation of Bcl10 was inhibited by the p38 stress-activated protein kinase inhibitors SB203580 and PD169316, suggesting that p38 is required for UV-mediated phosphorylation of Bcl10. (C) 2003 Elsevier Science (USA). All rights reserved.

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收藏

页码：923 / 926

页数：4

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