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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, 2008May 9, 2008; DOI 10.1182/blood-2007-11-121699.

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Submitted November 2, 2007
Accepted April 1, 2008

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

Inka Zschiedrich, Ulrike Hardeland, Anja Krones-Herzig, Mauricio Berriel Diaz, Alexandros Vegiopoulos, Johannes Muggenburg, Dirk Sombroek, Thomas G Hofmann, Rainer Zawatzky, Xiaolei Yu, Norbert Gretz, Mark Christian, Roger White, Malcolm G Parker, and Stephan Herzig*

Molecular Metabolic Control, German Cancer Research Center, Heidelberg, Germany
Cellular Senescence, German Cancer Research Center, Heidelberg, Germany
Viral Transformation Mechanisms, German Cancer Research Center, Heidelberg, Germany
Medical Research Center, Klinikum Mannheim, Mannheim, Germany
Institute of Reproductive and Developmental Biology, Imperial College, London, United Kingdom

* Corresponding author; email: s.herzig{at}dkfz.de.

Inflammatory responses represent a hallmark of numerous pathologies including sepsis, bacterial infection, insulin resistance, and malign obesity. Here we describe an unexpected co-activator function for the nuclear receptor interacting protein (RIP) 140 for nuclear factor (NF) kB, 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 pro-inflammatory 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 CREB-binding protein (CBP). RIP140-dependent control of pro-inflammatory gene expression via RelA/CBP may, therefore, represent a molecular rational for the cellular integration of metabolic and inflammatory pathways.


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