Peptide Hormones, Steroid Hormones, and Puffs: Mechanisms and Models in Insect Development

Henrich, Vincent C.; Rybczynski, Robert; Gilbert, Lawrence I.

doi:10.1016/s0083-6729(08)60934-6

Cited by 123 publications

(91 citation statements)

References 164 publications

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“…Steroids enter cells and bind to ligand-regulated transcription factors (Beato and Klug, 2000;Henrich, 1999). However, steroids also exert non-genomic effects that occur independently of gene transcription (Falkenstein et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

Solubilization of the Ecdysone Binding Protein from Anterior Silk Gland Cell Membranes of the Silkworm, Bombyx mori

Elmogy¹,

Iwami²,

Sakurai³

2007

Zoological Science

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We previously provided preliminary evidence for the presence of a putative membrane ecdysone receptor (mEcR) anchored in the plasma membranes of anterior silk glands (ASGs) in Bombyx mori. This receptor may act in concert with the conventional EcR in 20E-dependent programmed cell death of these glands. We report here, for the first time, the solubilization of mEcR from ASG membranes using the zwitterionic detergent CHAPS in the presence of NaCl. Our results show by ligand binding assay that mEcR solubilized this way is functionally active and retains 75% of its native binding activity. We also defined experimental conditions that yielded protein/detergent complexes with partial binding activity, which makes it possible to purify the membrane-bound ecdysone binding protein.

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Section: Introductionmentioning

confidence: 99%

Solubilization of the Ecdysone Binding Protein from Anterior Silk Gland Cell Membranes of the Silkworm, Bombyx mori

Elmogy¹,

Iwami²,

Sakurai³

2007

Zoological Science

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“…Different usage of EcR isoforms, the presence of specific co-regulators and co-factors and variation in structure and function of ecdysone response elements are thought to underlie the tissue-specific responses (e.g. Henrich et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

Ligand-dependent de-repression via EcR/USP acts as a gate to coordinate the differentiation of sensory neurons in theDrosophilawing

et al. 2005

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“…genes that were originally identified as ecdysone-inducible puffs in the larval salivary gland polytene chromosomes (Ashburner et al, 1974;Thummel, 1996;Richards, 1997;Henrich et al, 1999;Riddiford et al, 2001). These include E74, which encodes two related proteins that share a Cterminal ETS DNA binding domain, E74A and E74B (Burtis et al, 1990), and E75, which encodes three orphan members of the nuclear receptor superfamily, E75A, E75B and E75C (NR1D3) (Segraves and Hogness, 1990).…”

Section: Introductionmentioning

confidence: 99%

“…These include E74, which encodes two related proteins that share a Cterminal ETS DNA binding domain, E74A and E74B (Burtis et al, 1990), and E75, which encodes three orphan members of the nuclear receptor superfamily, E75A, E75B and E75C (NR1D3) (Segraves and Hogness, 1990). The early ecdysoneinducible transcription factors coordinate the expression of numerous secondary-response late genes that are responsible for directing appropriate stage-and tissue-specific biological responses during development (Thummel, 1996;Richards, 1997;Henrich et al, 1999;Riddiford et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

rigor mortisencodes a novel nuclear receptor interacting protein required for ecdysone signaling duringDrosophilalarval development

et al. 2004

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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 βFTZ-F1mutants. 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 βFTZ-F1. The ligand binding domain of βFTZ-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.

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Peptide Hormones, Steroid Hormones, and Puffs: Mechanisms and Models in Insect Development

Cited by 123 publications

References 164 publications

Solubilization of the Ecdysone Binding Protein from Anterior Silk Gland Cell Membranes of the Silkworm, Bombyx mori

Solubilization of the Ecdysone Binding Protein from Anterior Silk Gland Cell Membranes of the Silkworm, Bombyx mori

Ligand-dependent de-repression via EcR/USP acts as a gate to coordinate the differentiation of sensory neurons in theDrosophilawing

rigor mortisencodes a novel nuclear receptor interacting protein required for ecdysone signaling duringDrosophilalarval development

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