Gene regulation by thyroid hormone receptors

Current Opinion in Endocrinology and Diabetes

Volumn 3, Issue 5, 1996, Pages 412-416

  Horlein, Andreas J ^a   Heinzel, Thorsten ^a   Rosenfeld, Michael G ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0000728530     PISSN: 10683097     EISSN: None     Source Type: Journal    
DOI: 10.1097/00060793-199610000-00009     Document Type: Article

References (40)

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35. Lee JW, Ryan F, Swaffield JC, Johnston SA, Moore DD: Interaction of thyroid-hormone receptor with a conserved transcriptional mediator. Nature 1995, 374:91-94. Proteins that interact with the thyroid hormone receptor in a ligand-dependent fashion are identified using a two-hybrid screen. The authors concentrate on a specific clone whose product also interacts with RXR in presence of 9-cis retinoic acid. This protein, Trip1, has significant similarities to the yeast protein SUG-1. SUG-1 is a transcriptional mediator that interacts with transcriptional activation domains as well as the TATA binding protein TBP in vitro. The authors show that Trip1 can functionally substitute SUG-1 in a mutant yeast strain, in which SUG-1 expression is controlled by the glucose-repressible GAL promoter, indicating that Trip1 and SUG-1 are functionally related proteins.
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37. On̄ate SA, Tsai SY, Tsai M-J, O'Malley BW: Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science 1995, 270:1354-1357. Utilizing a two-hybrid screen the cDNA coding for a 110-kD protein, SRC-1 (for Steroid receptor coactivator 1), is identified that interacts with the progesterone receptor ligand-binding domain in the presence of ligand. In transfection experiments SRC-1 is able to stimulate levels of ligand-dependent transcription when cotransfected with PR, GR, ER, TR, and even RXR. An amino-terminally truncated version of SRC-1 acts as dominant-negative repressor. Together, these results suggest that SRC-1 is a general coactivator for members of the nuclear receptor superfamily and that it is likely to be one component of an active coactivator complex.
38. Cavailles V, Dauvois S, L'Horset F, Lopez G, Hoare S, Kushner PJ, Parker MG: Nuclear factor RIP140 modulates transcriptional activation by the estrogen receptor. EMBO J 1995, 14:3741-3751.
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