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J Biol Chem, Vol. 274, Issue 50, 35297-35300, December 10, 1999

COMMUNICATION
COP9 Signalosome-directed c-Jun Activation/Stabilization Is Independent of JNK^*

Michael Naumann^§, Dawadschargal Bech-Otschir^¶, Xiaohua Huang^¶, Katherine Ferrell^¶, and Wolfgang Dubiel^¶

From the  Max-Planck-Institut für Infektionsbiologie, Abteilung Molekulare Biologie and the ^¶ Institute of Biochemistry, Medical Faculty Charité, Humboldt University, 10117 Berlin, Germany

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.

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^* This work was supported by grants DU 229/5-1 (to W. D.) and Na 292/5-1 (to M. N.) from the Deutsche Forschungsgemeinschaft.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EMBL Data Bank with accession number(s) AF084260.

^§ To whom correspondence should be addressed. Tel.: 49 30 28460 410; Fax: 49 30 28460 401; E-mail: naumann@mpiib-berlin.mpg.de.

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Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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