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Journal of Biochemistry Advance Access originally published online on February 21, 2007
Journal of Biochemistry 2007 141(5):635-640; doi:10.1093/jb/mvm066
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© 2007 The Japanese Biochemical Society.

Characterization of the PC4 Binding Domain and its Interactions with HNF4{alpha}

Hongtao Guo, Chengjiang Gao, Zhiyong Mi, Jinping Zhang and Paul C. Kuo*

Deparment of Surgery, Duke University Medical Center, Durham, NC, USA

*To whom correspondence should be addressed. Tel: 919-668-1856, Fax: 919-684-8716, E-mail: kuo00004{at}mc.duke.edu

Received January 22, 2007; Accepted February 13, 2007


  Abstract

In the presence of oxidative stress, the hepatocellular inflammatory-redox (IR) state upregulates inducible nitric oxide synthase (iNOS) expression as an anti-oxidant function. In IL-1ß and peroxide treated hepatocytes, we have identified hepatocyte nuclear factor-4{alpha} (HNF4) and the transcriptional co-activator, PC4, to be essential for upregulation of iNOS transcription in this setting. The co-activator, PC4, facilitates activator-dependent transcription via interactions with basal transcriptional machinery that are independent of PC4-DNA binding. The interaction between HNF4 and PC4 has not been previously characterized. In this study utilizing human HepG2 cells, we demonstrate the critical role for p38 MAP kinase mediated HNF4 Ser158 phosphorylation (P-HNF4-S158), binding of PC4 to P-HNF4-S158 and characterize the functional domain of PC4 required for P-HNF4-S158 binding. Our results indicate that the presence of the IR state enhances PC4-HNF4 binding to upregulate transcription of target hepatocyte genes, such as iNOS.

Key Words: co-activator, inflammation, nitric oxide, nuclear receptor

Abbreviations: ChIP, chromatin immunoprecipitation; HNF4, hepatocyte nuclear factor 4-alpha; IL-1, interleukin 1ß; iNOS, inducible nitric oxide synthase; IR, inflammatory-redox; MM, mismatch; NO, nitric oxide; PCR, polymerase chain reaction; WT, wild type


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