Proceedings of the National Academy of Sciences - PNAS, 1995-08, Vol.92 (17), p.7966-7970
1995
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- Autor(en) / Beteiligte
- Titel
- Drosophila hormone receptor 38: a second partner for Drosophila USP suggests an unexpected role for nuclear receptors of the nerve growth factor-induced protein B type
- Ist Teil von
- Proceedings of the National Academy of Sciences - PNAS, 1995-08, Vol.92 (17), p.7966-7970
- Ort / Verlag
- United States: National Academy of Sciences of the United States of America
- Erscheinungsjahr
- 1995
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- In Drosophila the response to the hormone ecdysone is mediated in part by Ultraspiracle (USP) and ecdysone receptor (EcR), which are members of the nuclear receptor superfamily. Heterodimers of these proteins bind to ecdysone response elements (EcREs) and ecdysone to modulate transcription. Herein we describe Drosophila hormone receptor 38 (DHR38) and Bombyx hormone receptor 38 (BHR38), two insect homologues of rat nerve growth factor-induced protein B (NGFI-B). Although members of the NGFI-B family are thought to function exclusively as monomers, we show that DHR38 and BHR38 in fact interact strongly with USP and that this interaction is evolutionarily conserved. DHR38 can compete in vitro against EcR for dimerization with USP and consequently disrupt EcR-USP binding to an EcRE. Moreover, transfection experiments in Schneider cells show that DHR38 can affect ecdysone-dependent transcription. This suggests that DHR38 plays a role in the ecdysone response and that more generally NGFI-B type receptors may be able to function as heterodimers with retinoid X receptor type receptors in regulating transcription.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0027-8424eISSN: 1091-6490DOI: 10.1073/pnas.92.17.7966Titel-ID: cdi_proquest_miscellaneous_77458922
- Format
- –
- Schlagworte
- ADN, Amino Acid Sequence, Animals, Antibodies, Biology, Bombyx - metabolism, BOMBYX MORI, Cell Line, Cell Nucleus - metabolism, COMPOSICION QUIMICA, COMPOSITION CHIMIQUE, DNA, DNA-Binding Proteins - biosynthesis, DNA-Binding Proteins - chemistry, DNA-Binding Proteins - metabolism, Drosophila, Drosophila - metabolism, DROSOPHILA MELANOGASTER, Drosophila melanogaster - metabolism, Drosophila Proteins, Ecdysone - metabolism, ErbB Receptors - metabolism, GENETICA, GENETIQUE, HORMONAS DE LA MUDA, HORMONE DE MUE, Hormone receptors, Hormones, Insect genetics, Insect Hormones - biosynthesis, Insect Hormones - chemistry, Insect Hormones - metabolism, Insects, Molecular Sequence Data, Nerve Growth Factors - pharmacology, Nuclear receptors, Polymerase Chain Reaction, Protein Kinases, PROTEINAS, PROTEINE, Proteins, RECEPTEUR D'HORMONE, RECEPTORES DE HORMONAS, Receptors, Receptors, Cell Surface - biosynthesis, Receptors, Cell Surface - chemistry, Receptors, Cell Surface - metabolism, Receptors, Cytoplasmic and Nuclear, Receptors, Invertebrate Peptide - metabolism, Receptors, Steroid - metabolism, Recombinant Fusion Proteins - biosynthesis, Recombinant Fusion Proteins - chemistry, Recombinant Fusion Proteins - metabolism, SECUENCIA NUCLEICA, Sequence Homology, Amino Acid, SEQUENCE NUCLEIQUE, Transcription Factors - metabolism, Transfection, Vertebrates