Dimerization modulates the activity of the orphan nuclear receptor ERRgamma.

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Huppunen J, Aarnisalo P

Dimerization modulates the activity of the orphan nuclear receptor ERRgamma.

Biochem Biophys Res Commun. 2004 Feb 20;314(4):964-70.

PubMed ID

14751226 [ View in PubMed

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Abstract

Estrogen-related receptor gamma (ERRgamma) is an orphan nuclear receptor lacking identified natural ligands. However, 4-hydroxytamoxifen and diethylstilbestrol were recently shown to bind to and inhibit ERRgamma activity. ERR activates transcription constitutively as a monomer. We show here that ERRgamma forms also dimers via its ligand-binding domain. Homodimerization enhances the transcriptional activity. In contrast, heterodimerization with the related receptor ERRalpha inhibits the activities of both ERRgamma and ERRalpha. The inverse ERRgamma agonist 4OHT further inhibits the activity of the ERRgamma-ERRalpha heterodimer, indicating that 4OHT may modulate ERRalpha signaling via ERRgamma. Receptor dimerization thus modulates the transcriptional activities of ERRs.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Afimoxifene	Steroid hormone receptor ERR1	Protein	Humans	Unknown	Inhibitor	Details