The Nuclear Hormone Receptor NHR-40 Acts Downstream of the Sulfatase EUD-1 as Part of a Developmental Plasticity Switch in Pristionchus

AbstractEnvironment shapes development through a phenomenon called developmental plasticity. Deciphering its genetic basis has implications for understanding evolution and adaptation to novel environments, yet molecular studies are scarce. Here, we expanded the gene regulatory network controlling predatory vs. non-predatory morphology in the nematode Pristionchus pacificus. First, we isolated a mutant in the nuclear hormone receptor nhr-1 with a previously unseen phenotypic effect. It disrupts mouth-form determination and results in animals combining features of both wild-type morphs. Further, we identified common targets of NHR-1 and the previously identified nuclear hormone receptor NHR-40 through transcriptomics. Unlike their highly conserved regulators, the target genes have no orthologs in Caenorhabditis elegans and likely result from lineage-specific expansions. An array of transcriptional reporters revealed co-expression of all tested targets in the same pharyngeal gland cell. The morphological remodeling of this cell accompanied the evolution of teeth and predation, linking rapid gene turnover with morphological innovations.

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Faculty Opinions recommendation of Regulation of C. elegans fat uptake and storage by acyl-CoA synthase-3 is dependent on NR5A family nuclear hormone receptor nhr-25.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.7660956.7972054 ◽

2011 ◽

Author(s):

Joel Elmquist ◽

Kevin Williams

Keyword(s):

Hormone Receptor ◽

Nuclear Hormone Receptor ◽

C Elegans ◽

Fat Uptake ◽

And Storage

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Intermittent Expression of BmFTZ-F1, a Member of the Nuclear Hormone Receptor Superfamily during Development of the Silkworm Bombyx mori

Developmental Biology ◽

10.1006/dbio.1994.1099 ◽

1994 ◽

Vol 162 (2) ◽

pp. 426-437 ◽

Cited By ~ 80

Author(s):

Guan-Cheng Sun ◽

Susumu Hirose ◽

Hitoshi Ueda

Keyword(s):

Bombyx Mori ◽

Hormone Receptor ◽

Nuclear Hormone Receptor ◽

Silkworm Bombyx Mori

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Phosphorylation of the Hinge Domain of the Nuclear Hormone Receptor LRH-1 Stimulates Transactivation

Journal of Biological Chemistry ◽

10.1074/jbc.m509115200 ◽

2006 ◽

Vol 281 (12) ◽

pp. 7850-7855 ◽

Cited By ~ 62

Author(s):

Yoon-Kwang Lee ◽

Yun-Hee Choi ◽

Steven Chua ◽

Young Joo Park ◽

David D. Moore

Keyword(s):

Hormone Receptor ◽

Nuclear Hormone Receptor ◽

Hinge Domain

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Pseudoginsenoside F11, a Novel Partial PPARγAgonist, Promotes Adiponectin Oligomerization and Secretion in 3T3-L1 Adipocytes

PPAR Research ◽

10.1155/2013/701017 ◽

2013 ◽

Vol 2013 ◽

pp. 1-8 ◽

Cited By ~ 17

Author(s):

Guoyu Wu ◽

Junyang Yi ◽

Ling Liu ◽

Pengcheng Wang ◽

Zhijie Zhang ◽

...

Keyword(s):

Type 2 Diabetes ◽

Side Effects ◽

Hormone Receptor ◽

Adipocyte Differentiation ◽

American Ginseng ◽

Nuclear Hormone Receptor ◽

Targeted Therapeutics ◽

Panax Quinquefolium ◽

Master Regulator

PPARγis a nuclear hormone receptor that functions as a master regulator of adipocyte differentiation and development. Full PPARγagonists, such as the thiazolidinediones (TZDs), have been widely used to treat type 2 diabetes. However, they are characterized by undesirable side effects due to their strong agonist activities. Pseudoginsenoside F11 (p-F11) is an ocotillol-type ginsenoside isolated fromPanax quinquefolium L.(American ginseng). In this study, we found that p-F11 activates PPARγwith modest adipogenic activity. In addition, p-F11 promotes adiponectin oligomerization and secretion in 3T3-L1 adipocytes. We also found that p-F11 inhibits obesity-linked phosphorylation of PPARγat Ser-273 by Cdk5. Therefore, p-F11 is a novel partial PPARγagonist, which might have the potential to be developed as a new PPARγ-targeted therapeutics for type 2 diabetes.

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