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First published online 26 November 2003
doi: 10.1242/dev.00920

Development 131, 25-36 (2004)
Published by The Company of Biologists 2004
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rigor mortis encodes a novel nuclear receptor interacting protein required for ecdysone signaling during Drosophila larval development

Julie Gates1,*, Geanette Lam1, José A. Ortiz2, Régine Losson3 and Carl S. Thummel1,{dagger}

1 Howard Hughes Medical Institute, Department of Human Genetics, University of Utah School of Medicine, Salt Lake City, UT 84112-5331 USA
2 Instituto de Neurociencias, Universidad Miguel Hernández-CSIC, Apdo.18, Ctra. Valencia Km 87, 03550-San Juan (Alicante), Spain
3 IGBMC, Dépt de Génétique Physiologique, BP 10142, 67404 Illkirch Cedex, CU Strasbourg, France

{dagger} Author for correspondence (e-mail: carl.thummel{at}genetics.utah.edu)

Accepted 8 October 2003

Pulses of the steroid hormone ecdysone trigger the major developmental transitions in Drosophila, including molting and puparium formation. The ecdysone signal is transduced by the EcR/USP nuclear receptor heterodimer that binds to specific response elements in the genome and directly regulates target gene transcription. We describe a novel nuclear receptor interacting protein encoded by rigor mortis (rig) that is required for ecdysone responses during larval development. rig mutants display defects in molting, delayed larval development, larval lethality, duplicated mouth parts, and defects in puparium formation – phenotypes that resemble those seen in EcR, usp, E75A and ßFTZ-F1 mutants. Although the expression of these nuclear receptor genes is essentially normal in rig mutant larvae, the ecdysone-triggered switch in E74 isoform expression is defective. rig encodes a protein with multiple WD-40 repeats and an LXXLL motif, sequences that act as specific protein-protein interaction domains. Consistent with the presence of these elements and the lethal phenotypes of rig mutants, Rig protein interacts with several Drosophila nuclear receptors in GST pull-down experiments, including EcR, USP, DHR3, SVP and ßFTZ-F1. The ligand binding domain of ßFTZ-F1 is sufficient for this interaction, which can occur in an AF-2-independent manner. Antibody stains reveal that Rig protein is present in the brain and imaginal discs of second and third instar larvae, where it is restricted to the cytoplasm. In larval salivary gland and midgut cells, however, Rig shuttles between the cytoplasm and nucleus in a spatially and temporally regulated manner, at times that correlate with the major lethal phase of rig mutants and major switches in ecdysone-regulated gene expression. Taken together, these data indicate that rig exerts essential functions during larval development through gene-specific effects on ecdysone-regulated transcription, most likely as a cofactor for one or more nuclear receptors. Furthermore, the dynamic intracellular redistribution of Rig protein suggests that it may act to refine spatial and temporal responses to ecdysone during development.

Key words: Nuclear receptor, Hormone, Cofactor, Ecdysone, Molting


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