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 Blood, 15 July 2008, Vol. 112, No. 2, pp. 264-276.
Prepublished online as a Blood First Edition Paper on May 9, 2008; DOI 10.1182/blood-2007-11-121699.

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CHEMOKINES, CYTOKINES, AND INTERLEUKINS

Coactivator function of RIP140 for NF{kappa}B/RelA-dependent cytokine gene expression

Inka Zschiedrich1, Ulrike Hardeland1, Anja Krones-Herzig1, Mauricio Berriel Diaz1, Alexandros Vegiopoulos1, Johannes Müggenburg1, Dirk Sombroek2, Thomas G. Hofmann2, Rainer Zawatzky3, Xiaolei Yu4, Norbert Gretz4, Mark Christian5, Roger White5, Malcolm G. Parker5, and Stephan Herzig1

1 Emmy Noether and Marie Curie Research Group Molecular Metabolic Control, 2 Research Group Cellular Senescence, and 3 Department of Viral Transformation Mechanisms, German Cancer Research Center Heidelberg, Heidelberg, Germany; 4 Medical Research Center, Klinikum Mannheim, Mannheim, Germany; and 5 Institute of Reproductive and Developmental Biology, Imperial College London, Faculty of Medicine, London, United Kingdom

Inflammatory responses represent a hallmark of numerous pathologies including sepsis, bacterial infection, insulin resistance, and malign obesity. Here we describe an unexpected coactivator function for the nuclear receptor interacting protein 140 (RIP140) for nuclear factor {kappa}B (NF{kappa}B), a master transcriptional regulator of inflammation in multiple tissues. Previous work has shown that RIP140 suppresses the expression of metabolic gene networks, but we have found that genetic as well as acute deficiency of RIP140 leads to the inhibition of the proinflammatory program in macrophages. The ability of RIP140 to function as a coactivator for cytokine gene promoter activity relies on direct protein-protein interactions with the NF{kappa}B subunit RelA and histone acetylase cAMP-responsive element binding protein (CREB)-binding protein (CBP). RIP140-dependent control of proinflammatory gene expression via RelA/CBP may, therefore, represent a molecular rational for the cellular integration of metabolic and inflammatory pathways.


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