Sterol regulatory element-binding protein-1 interacts with the nuclear thyroid hormone receptor to enhance acetyl-CoA carboxylase-alpha transcription in hepatocytes

The Journal of Biological Chemistry
Liya YinF B Hillgartner

Abstract

In previous work, we characterized a 3,5,3'-triiodothyronine response element (T3RE) in acetyl-CoA carboxylase-alpha (ACCalpha) promoter 2 that mediated 3,5,3'-triiodothyronine (T3) regulation of ACCalpha transcription in chick embryo hepatocytes. Sequence comparison analysis revealed the presence of sterol regulatory element-1 (SRE-1) located 5 bp downstream of the ACCalpha T3RE. Here, we investigated the role of this SRE-1 in modulating T3 regulation of ACCalpha transcription. Transfection analyses demonstrated that the SRE-1 enhanced T3-induced ACCalpha transcription by more than 2-fold in hepatocytes. The effect of the SRE-1 on T3 responsiveness required the presence of the T3RE in its native orientation. In pull-down experiments, the mature form of sterol regulatory element-binding protein-1 (SREBP-1) specifically bound the alpha-isoform of the nuclear T3 receptor (TR), and the presence of T3 enhanced this interaction. A region of TRalpha containing the DNA-binding domain plus flanking sequences (amino acids 21-157) was required for interaction with SREBP-1, and a region of SREBP-1 containing the basic helix-loop-helix-leucine zipper domain (amino acids 300-389) was required for interaction with TRalpha. In gel mobility sh...Continue Reading

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