Literature DB >> 8163464

A novel heterodimerization partner for thyroid hormone receptor. Peroxisome proliferator-activated receptor.

F Bogazzi1, L D Hudson, V M Nikodem.   

Abstract

Retinoid-like receptors play a central role in hormonal responses by forming heterodimers with other nuclear hormone receptors. In this study we have identified the peroxisome proliferator-activated receptor (PPAR) as a new thyroid hormone receptor (THR) auxiliary nuclear protein, heterodimerizing with THR in solution. Although these heterodimers do not recognize a classical thyroid hormone response element (TRE) characterized by direct repeat separated by four nucleotides (DR+4), PPAR behaves as a dominant negative regulator of thyroid hormone (TH) action. However, a TH-dependent positive effect is elicited by selective interaction of the THR beta-PPAR but not the THR alpha-PPAR heterodimer with a novel TRE (DR+2). The critical region of THR beta was mapped to 3 amino acids in the distal box of the DNA binding domain. Hence, PPAR can positively or negatively influence TH action depending on TRE structure and THR isotype.

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Year:  1994        PMID: 8163464

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  23 in total

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Authors:  C W Wong; M L Privalsky
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8.  Phosphorylation enhances the target gene sequence-dependent dimerization of thyroid hormone receptor with retinoid X receptor.

Authors:  M K Bhat; K Ashizawa; S Y Cheng
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Review 9.  Expression of thyroid hormone receptor isoforms in the oligodendrocyte lineage.

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10.  Thyroid hormone (T3) inhibits ciprofibrate-induced transcription of genes encoding beta-oxidation enzymes: cross talk between peroxisome proliferator and T3 signaling pathways.

Authors:  R Chu; L D Madison; Y Lin; P Kopp; M S Rao; J L Jameson; J K Reddy
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