COP9 signalosome-directed c-Jun activation/stabilization is independent of JNK

被引:121
作者
Naumann, M [1 ]
Bech-Otschir, D
Huang, XH
Ferrell, K
Dubiel, W
机构
[1] Max Planck Inst Infekt Biol, Mol Biol Abt, D-10117 Berlin, Germany
[2] Humboldt Univ, Med Fac Charite, Inst Biochem, D-10117 Berlin, Germany
关键词
D O I
10.1074/jbc.274.50.35297
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 basic region-leucine zipper transcription factor c-Jun regulates gene expression and cell function. It participates in the formation of homo- or heterodimeric complexes that specifically bind to DNA sequences called activating protein 1 (AP-1) sites, The stability and activity of c-Jun is regulated by phosphorylation within the N-terminal activation domain. Mitogen- and stress-activated c-Jun N-terminal kinases (JNKs) were previously the only described enzymes phosphorylating c-Jun at the N terminus in vivo. In this report we demonstrate a JNK-independent activation of c-Jun in vivo directed by the constitutive photomorphogenesis (COP9) signalosome. The overexpression of signalosome subunit 2 (Sgn2), a subunit of the COP9 signalosome, leads to de novo assembly of the complex with a partial incorporation of the overexpressed subunit, The de novo formation of COP9 signalosome parallels an increase of c-Jun protein resulting in elevated AP-1 transcriptional activity. The c-Jun activation caused by Sgn2 overexpression is independent of JNK and mitogen-activated protein kinase kinase 4. The data demonstrate the existence of a novel COP9 signalosome-directed c-Jun activation pathway.
引用
收藏
页码:35297 / 35300
页数:4
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