Heterodimerization of the Drosophila ecdysone receptor with retinoid X receptor and ultraspiracle

Helen E. Thomas, Hendrik G. Stunnenberg, A. Francis Stewart

Research output: Contribution to journalArticlepeer-review

458 Citations (Scopus)

Abstract

ECDYSONE in Drosophila has been a paradigm for steroid hormones since its ability to induce gene activity directly was demonstrated by its effects on moulting and polytene chromosome puffing1-3. The ecdysone receptor (EcR) was recently confirmed as a member of the nuclear receptor superfamily by cloning and characterization in a Drosophila cell line4. Here we show that EcR needs to heterodimerize with either the retinoid X receptor (RXR)5 or its Drosophila homologue, ultraspiracle (USP)6, for DNA binding and transactivation. These results place the ecdysone receptor in the heterodimerizing class of the nuclear receptor superfamily and demonstrate that the role of RXR/USP as a central and promiscuous partner in mediating the activity of these receptors7-12 is highly conserved. Whereas EcR-USP DNA-binding activity is unaffected by hormone, EcR-RXR DNA-binding activity is stimulated by either ecdysteroid or 9-cis-retinoic acid, demonstrating that hormone can play a role in heterodimer stabilization.

Original languageEnglish
Pages (from-to)471-475
Number of pages5
JournalNature
Volume362
Issue number6419
DOIs
Publication statusPublished - 1993
Externally publishedYes

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