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A more recent version of this article appeared on August 1, 2004

Papers In Press, published online ahead of print May 16, 2004
J. Lipid Res., doi:10.1194/jlr.M400088-JLR200
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Submitted on March 2, 2004
Revised on May 11, 2004
Accepted on May 13, 2004

Phorbolester promotes histone H3-Ser10 phosphorylation at low density lipoprotein receptor promoter in a protein kinase C-dependent manner in human hepatoma HepG2 cells

Wei Huang, Vachaspati Mishra, Sanjay Batra, Ishan Dillon, and Kamal D. Mehta

Molecular and Cellular Biochemistry, Ohio State University College of Medicine and Public Health, Columbus, Ohio 43210

Corresponding Author: mehta.80{at}osu.edu

Histone modification is emerging as a major regulatory mechanism for modulating gene expression by altering the accessibility of transcription factors to DNA. This study unravels the relationship between histone H3 modifications and LDL receptor induction, focusing also on routes by which phosphorylation is mediated in human hepatoma HepG2 cells. We show that while histone H3 is constitutively acetylated at LDL receptor chromatin, 12-O-tetradecanoylphorbol-13-acetate (TPA) causes rapid hyperphosphorylation of histone H3 on Serine 10 (histone H3-Ser10), despite global reduction in its phosphorylation levels. Ser10 hyperphosphorylation precedes LDL receptor induction, and is independent of p42/44MAPK, p38MAPK, pp90RSK, or MSK-1 cascade. Interestingly, inhibition of protein kinase C (PKC) blocks Ser10 hyperphosphorylation and also compromises LDL receptor induction by TPA. Consistent with its role, recombinant purified PKC indeed phosphorylate purified histone H3 on Ser10. Collectively, our findings highlight a novel role for PKC in regulating histone H3-Ser10 phosphorylation, and suggest that histone modification, together with promoter specific architecture, provides numerous regulatory opportunities to set the overall range of control attainable for LDL receptor gene induction.


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