Selective association of sterol regulatory element-binding protein isoforms with target promoters in vivo.

The Journal of Biological Chemistry
Mary K BennettT F Osborne

Abstract

The mRNAs for all three members of the sterol regulatory element-binding protein (SREBP) family are widely expressed, and the proteins are highly similar. They have potential to both hetero- and homodimerize through their bHLHLZ domains, so it has been difficult to definitively study the role of each one apart from the other two. In the current study, we have utilized cell lines that express only one functional SREBP and the chromatin immunoprecipitation technique to analyze individual SREBP binding to three specific target genes: hydroxymethylglutaryl-CoA reductase (Red), fatty acid synthase (FAS), and squalene synthase (SQS). Our studies show that SREBP-2 binds to promoters for all three genes, and in agreement with the original report using these cells, all three mRNAs are also induced. In the line expressing only SREBP-1a, mRNAs for Red and FAS are induced, but SQS is not. Chromatin immunoprecipitation also shows that SREBP-1a is recruited efficiently to Red and FAS promoters but not to SQS. This observation indicates SREBP-2 selectively binds the SQS promoter and is sufficient to explain the lack of SQS mRNA induction in the SREBP-1a-expressing cells. SREBP-1c protein was not stably recruited to any SREBP target promoter d...Continue Reading

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Citations

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Mar 18, 2008·Chemistry and Physics of Lipids·Donald B JumpBarbara Christian
Sep 13, 2005·Biochimica Et Biophysica Acta·Thomas Klaus FelderHannes Oberkofler
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Sep 8, 2006·Journal of Lipid Research·Karen E MatsukumaTimothy F Osborne
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Aug 30, 2005·The Journal of Biological Chemistry·William R LagorGene C Ness
Oct 28, 2005·The Journal of Nutrition·Donald B JumpOlivier Demeure
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