Constitutive Activation of Transcription and Binding of Coactivator by Estrogen-Related Receptors 1 and 2 | Zendy

Wen Xie | Zendy; Heng Hong | Zendy; Na Yang | Zendy; Richard J. Lin | Zendy; Cynthia M. Simon | Zendy; Michael R. Stallcup | Zendy; Ronald M. Evans | Zendy

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Constitutive Activation of Transcription and Binding of Coactivator by Estrogen-Related Receptors 1 and 2

Author(s) -

Wen Xie,

Heng Hong,

Na Yang,

Richard J. Lin,

Cynthia M. Simon,

Michael R. Stallcup,

Ronald M. Evans

Publication year - 1999

Publication title -

molecular endocrinology

Language(s) - English

Resource type - Journals

eISSN - 1944-9917

pISSN - 0888-8809

DOI - 10.1210/mend.13.12.0381

Subject(s) - nuclear receptor coactivator 3 , nuclear receptor , nuclear receptor coactivator 1 , hormone response element , pelp 1 , nuclear receptor coactivator 2 , estrogen related receptor gamma , coactivator , biology , estrogen receptor , receptor , thyroid hormone receptor , response element , nuclear receptor co repressor 1 , steroid hormone , microbiology and biotechnology , glucocorticoid receptor , estrogen receptor beta , transcription factor , biochemistry , genetics , gene , gene expression , promoter , cancer , breast cancer

In this report, we demonstrate that, in contrast to most previously characterized nuclear receptors, hERR1 and hERR2 (human estrogen receptor-related protein 1 and -2) are constitutive activators of the classic estrogen response element (ERE) as well as the palindromic thyroid hormone response element (TRE(pal)) but not the glucocorticoid response element (GRE). This intrinsically activated state of hERR1 and hERR2 resides in the ligand-binding domains of the two genes and is transferable to a heterologous receptor. In addition, we show that members of the p160 family of nuclear receptor coactivators, ACTR (activator of thyroid and retinoic acid receptors), GRIP1 (glucocorticoid receptor interacting protein 1), and SRC-1 (steroid receptor coactivator 1), potentiate the transcriptional activity by hERR1 and hERR2 in mammalian cells, and that both orphan receptors bind the coactivators in a ligand-independent manner. Together, these results suggest that hERR1 and hERR2 activate gene transcription through a mechanism different from most of the previously characterized steroid hormone receptors.

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