Drosophila ultraspiracle modulates ecdysone receptor function via heterodimer formation.
The vertebrate retinoid X receptor (RXR) has been implicated in the regulation of multiple hormonal signaling pathways through the formation of heteromeric receptor complexes that bind DNA with high affinity. We now demonstrate that ultraspiracle (usp), a Drosophila RXR homolog, can substitute for RXR in stimulating the DNA binding of receptors for retinoic acid, T3, vitamin D, and peroxisome proliferator activators. These observations led to the search and ultimate identification of the ecdysone receptor (EcR) as a Drosophila partner of usp. Together, usp and EcR bind DNA in a highly cooperative fashion. Cotransfection of both EcR and usp expression vectors is required to render cultured mammalian cells ecdysone responsive. These results implicate usp as an integral component of the functional EcR. By demonstrating that receptor heterodimer formation precedes the divergence of vertebrate and invertebrate lineages, these data underscore a central role for RXR and its homolog usp in the evolution and control of the nuclear receptor-based endocrine system.
Duke Scholars
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Related Subject Headings
- Transfection
- Transcription Factors
- Retinoid X Receptors
- Receptors, Steroid
- Receptors, Retinoic Acid
- Receptors, Cell Surface
- Plasmids
- Nuclear Proteins
- Molecular Sequence Data
- Macromolecular Substances
Citation
Published In
DOI
ISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Transfection
- Transcription Factors
- Retinoid X Receptors
- Receptors, Steroid
- Receptors, Retinoic Acid
- Receptors, Cell Surface
- Plasmids
- Nuclear Proteins
- Molecular Sequence Data
- Macromolecular Substances