Source:http://linkedlifedata.com/resource/pubmed/id/16919260
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2006-10-2
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pubmed:abstractText |
C. elegans ahr-1 is orthologous to the mammalian aryl hydrocarbon receptor, and it functions as a transcription factor to regulate the development of certain neurons. Here, we describe the role of ahr-1 in a specific behavior: the aggregation of C. elegans on lawns of bacterial food. This behavior is modulated by nutritional cues and ambient oxygen levels, and aggregation is inhibited by the npr-1 G protein-coupled neuropeptide receptor gene. Loss-of-function mutations in ahr-1 or its transcription partner aha-1 (ARNT) suppress aggregation behavior in npr-1-deficient animals. This behavioral defect is not irreparable. Aggregation behavior can be restored to ahr-1-deficient animals by heat-shock induction of ahr-1 transcription several hours after ahr-1-expressing neurons have normally differentiated. We show that ahr-1 and aha-1 promote cell-type-specific expression of soluble guanylate cyclase genes that have key roles in aggregation behavior and hyperoxia avoidance. Aggregation behavior can be partially restored to ahr-1 mutant animals by expression of ahr-1 in only 4 neurons, including URXR and URXL. We conclude that the AHR-1:AHA-1 transcription complex regulates the expression of soluble guanylate cyclase genes and other unidentified genes that are essential for acute regulation of aggregation behavior.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DAF-21 protein, C elegans,
http://linkedlifedata.com/resource/pubmed/chemical/Guanylate Cyclase,
http://linkedlifedata.com/resource/pubmed/chemical/HSP90 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Aryl Hydrocarbon,
http://linkedlifedata.com/resource/pubmed/chemical/ahr-1 protein, C elegans
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0012-1606
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
298
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
606-15
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pubmed:meshHeading |
pubmed-meshheading:16919260-Animals,
pubmed-meshheading:16919260-Base Sequence,
pubmed-meshheading:16919260-Caenorhabditis elegans,
pubmed-meshheading:16919260-Caenorhabditis elegans Proteins,
pubmed-meshheading:16919260-Cell Aggregation,
pubmed-meshheading:16919260-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:16919260-Guanylate Cyclase,
pubmed-meshheading:16919260-HSP90 Heat-Shock Proteins,
pubmed-meshheading:16919260-Models, Biological,
pubmed-meshheading:16919260-Molecular Sequence Data,
pubmed-meshheading:16919260-Neurons,
pubmed-meshheading:16919260-Receptors, Aryl Hydrocarbon,
pubmed-meshheading:16919260-Solubility,
pubmed-meshheading:16919260-Transcription, Genetic
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pubmed:year |
2006
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pubmed:articleTitle |
The Caenorhabditis elegans AHR-1 transcription complex controls expression of soluble guanylate cyclase genes in the URX neurons and regulates aggregation behavior.
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pubmed:affiliation |
Department of Genetics, Development, and Cell Biology, 2108 Molecular Biology Building, Iowa State University, Ames, IA 50011-3260, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
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