CHR3: a Caenorhabditis elegans orphan nuclear hormone receptor required for proper epidermal development and molting

Development ◽  
1998 ◽  
Vol 125 (9) ◽  
pp. 1617-1626 ◽  
Author(s):  
M. Kostrouchova ◽  
M. Krause ◽  
Z. Kostrouch ◽  
J.E. Rall
Keyword(s):  
Caenorhabditis Elegans ◽  
Hormone Receptor ◽  
Nuclear Protein ◽  
Cell Function ◽  
Reporter Genes ◽  
Postembryonic Development ◽  
Nuclear Hormone Receptor ◽  
Hormone Response ◽  
Gene Encoding ◽  
Inducible Gene

CHR3 is a Caenorhabditis elegans orphan nuclear hormone receptor highly homologous to Drosophila DHR3, an ecdysone-inducible gene product involved in metamorphosis. Related vertebrate factors include RORalpha/RZRalpha, RZRbeta and RevErb. Gel-shift studies show that CHR3 can bind the DR5-type hormone response sequence. CHR3 is a nuclear protein present in all blastomeres during early embryogenesis. During morphogenesis, both CHR3 protein and zygotically active reporter genes are detectable in epidermal cells and their precursors. Inhibition of the gene encoding CHR3 results in several larval defects associated with abnormal epidermal cell function, including molting and body size regulation, suggesting that CHR3 is an essential epidermal factor required for proper postembryonic development.

scholarly journals Nuclear hormone receptor DHR96 mediates the resistance to xenobiotics but not the increased lifespan of insulin-mutant Drosophila

2016 ◽  
Vol 113 (5) ◽  
pp. 1321-1326 ◽  
Author(s):  
Sonita Afschar ◽  
Janne M. Toivonen ◽  
Julia Marianne Hoffmann ◽  
Luke Stephen Tain ◽  
Daniela Wieser ◽  
...  
Keyword(s):  
Hormone Receptor ◽  
Fruit Fly ◽  
Xenobiotic Metabolism ◽  
Nuclear Hormone Receptor ◽  
Laboratory Animals ◽  
Dietary Interventions ◽  
Gene Encoding ◽  
Transgenic Expression ◽  
C Elegans ◽  
Lipophilic Toxins

Lifespan of laboratory animals can be increased by genetic, pharmacological, and dietary interventions. Increased expression of genes involved in xenobiotic metabolism, together with resistance to xenobiotics, are frequent correlates of lifespan extension in the nematode worm Caenorhabditis elegans, the fruit fly Drosophila, and mice. The Green Theory of Aging suggests that this association is causal, with the ability of cells to rid themselves of lipophilic toxins limiting normal lifespan. To test this idea, we experimentally increased resistance of Drosophila to the xenobiotic dichlordiphenyltrichlorethan (DDT), by artificial selection or by transgenic expression of a gene encoding a cytochrome P450. Although both interventions increased DDT resistance, neither increased lifespan. Furthermore, dietary restriction increased lifespan without increasing xenobiotic resistance, confirming that the two traits can be uncoupled. Reduced activity of the insulin/Igf signaling (IIS) pathway increases resistance to xenobiotics and extends lifespan in Drosophila, and can also increase longevity in C. elegans, mice, and possibly humans. We identified a nuclear hormone receptor, DHR96, as an essential mediator of the increased xenobiotic resistance of IIS mutant flies. However, the IIS mutants remained long-lived in the absence of DHR96 and the xenobiotic resistance that it conferred. Thus, in Drosophila IIS mutants, increased xenobiotic resistance and enhanced longevity are not causally connected. The frequent co-occurrence of the two traits may instead have evolved because, in nature, lowered IIS can signal the presence of pathogens. It will be important to determine whether enhanced xenobiotic metabolism is also a correlated, rather than a causal, trait in long-lived mice.

scholarly journals Repression of a Potassium Channel by Nuclear Hormone Receptor and TGF-β Signaling Modulates Insulin Signaling in Caenorhabditis elegans

PLoS Genetics ◽  
2012 ◽  
Vol 8 (2) ◽  
pp. e1002519 ◽  
Author(s):  
Donha Park ◽  
Karen L. Jones ◽  
Hyojin Lee ◽  
Terrance P. Snutch ◽  
Stefan Taubert ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Potassium Channel ◽  
Insulin Signaling ◽  
Hormone Receptor ◽  
Nuclear Hormone Receptor

scholarly journals Gain-of-Function Alleles in Caenorhabditis elegans Nuclear Hormone Receptor nhr-49 Are Functionally Distinct

PLoS ONE ◽  
2016 ◽  
Vol 11 (9) ◽  
pp. e0162708 ◽  
Author(s):  
Kayoung Lee ◽  
Grace Ying Shyen Goh ◽  
Marcus Andrew Wong ◽  
Tara Leah Klassen ◽  
Stefan Taubert
Keyword(s):  
Caenorhabditis Elegans ◽  
Hormone Receptor ◽  
Nuclear Hormone Receptor ◽  
Gain Of Function

scholarly journals Caenorhabditis elegans methionine/S-adenosylmethionine cycle activity is sensed and adjusted by a nuclear hormone receptor

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Gabrielle E Giese ◽  
Melissa D Walker ◽  
Olga Ponomarova ◽  
Hefei Zhang ◽  
Xuhang Li ◽  
...  
Keyword(s):  
Gene Expression ◽  
Caenorhabditis Elegans ◽  
Vitamin B12 ◽  
Transcriptional Activation ◽  
Hormone Receptor ◽  
Metabolic Pathways ◽  
Nuclear Hormone Receptor ◽  
Dietary Vitamin ◽  
Independent Mechanism ◽  
Dependent Mechanism

Vitamin B12 is an essential micronutrient that functions in two metabolic pathways: the canonical propionate breakdown pathway and the methionine/S-adenosylmethionine (Met/SAM) cycle. In Caenorhabditis elegans, low vitamin B12, or genetic perturbation of the canonical propionate breakdown pathway results in propionate accumulation and the transcriptional activation of a propionate shunt pathway. This propionate-dependent mechanism requires nhr-10 and is referred to as ‘B12-mechanism-I’. Here, we report that vitamin B12 represses the expression of Met/SAM cycle genes by a propionate-independent mechanism we refer to as ‘B12-mechanism-II’. This mechanism is activated by perturbations in the Met/SAM cycle, genetically or due to low dietary vitamin B12. B12-mechanism-II requires nhr-114 to activate Met/SAM cycle gene expression, the vitamin B12 transporter, pmp-5, and adjust influx and efflux of the cycle by activating msra-1 and repressing cbs-1, respectively. Taken together, Met/SAM cycle activity is sensed and transcriptionally adjusted to be in a tight metabolic regime.

scholarly journals Ilex paraguariensis modulates fat metabolism in Caenorhabditis elegans through purinergic system (ADOR-1) and nuclear hormone receptor (NHR-49) pathways

PLoS ONE ◽  
2018 ◽  
Vol 13 (9) ◽  
pp. e0204023 ◽  
Author(s):  
Marina Lopes Machado ◽  
Leticia Priscilla Arantes ◽  
Priscila Gubert ◽  
Daniele Coradini Zamberlan ◽  
Thayanara Cruz da Silva ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Hormone Receptor ◽  
Fat Metabolism ◽  
Nuclear Hormone Receptor ◽  
Ilex Paraguariensis ◽  
Purinergic System

scholarly journals WITHDRAWN: Caenorhabditis elegans nuclear hormone receptor NHR-14, cooperates with p53/cep-1 to regulate DNA damage-induced apoptosis

Oncotarget ◽  
2018 ◽  
Vol 0 (0) ◽  
Author(s):  
Junling Shen ◽  
Jiaxin Kang ◽  
Zhuang Yao ◽  
Youli Jian ◽  
Yudong Jing ◽  
...  
Keyword(s):  
Dna Damage ◽  
Caenorhabditis Elegans ◽  
Hormone Receptor ◽  
Nuclear Hormone Receptor ◽  
Induced Apoptosis

scholarly journals The pseudouridine synthase dyskerin binds to cytoplasmic H/ACA-box snoRNA retaining transcripts affecting nuclear hormone receptor dependence

2021 ◽  
Author(s):  
Federico Zacchini ◽  
Giulia Venturi ◽  
Veronica De Sanctis ◽  
Roberto Bertorelli ◽  
Claudio Ceccarelli ◽  
...  
Keyword(s):  
Hormone Receptor ◽  
Nuclear Protein ◽  
Specific Activity ◽  
Nuclear Hormone Receptor ◽  
Transcriptional Networks ◽  
Receptor Ligands ◽  
Mrna Isoforms ◽  
Protein Coding ◽  
Pseudouridine Synthase ◽  
Cytoplasmic Ribosomes

ABSTRACTDyskerin is a nuclear protein involved in H/ACA box snoRNA-guided uridine modification of RNA. Since its defective function induces specific alterations in gene expression, we sought to unbiasedly identify mRNAs regulated by dyskerin. We found that dyskerin depletion affects the expression or the association with polysomes of selected mRNA isoforms characterized by the retention of H/ACA box snoRNA-containing introns. These snoRNA retaining transcripts (snoRTs) are bound by dyskerin and can interact with cytoplasmic ribosomes. We then characterized the cytoplasmic dyskerin RNA interactome finding both H/ACA box snoRTs and protein-coding transcripts. Since a fraction of these latter transcripts is involved in the nuclear hormone receptor binding, we tested to see if this specific activity is affected by dyskerin. Results indicate that dyskerin dysregulation may alter the dependence on nuclear hormone receptor ligands in breast cancer. Our work suggests a cytoplasmic function for dyskerin which could affect mRNA post-transcriptional networks relevant for nuclear hormone receptor functions.

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