rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6022
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pubmed:dateCreated |
2011-3-11
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pubmed:abstractText |
Many animals, including the fruit fly, are sensitive to small differences in ambient temperature. The ability of Drosophila larvae to choose their ideal temperature (18°C) over other comfortable temperatures (19° to 24°C) depends on a thermosensory signaling pathway that includes a heterotrimeric guanine nucleotide-binding protein (G protein), a phospholipase C, and the transient receptor potential TRPA1 channel. We report that mutation of the gene (ninaE) encoding a classical G protein-coupled receptor (GPCR), Drosophila rhodopsin, eliminates thermotactic discrimination in the comfortable temperature range. This role for rhodopsin in thermotaxis toward 18°C was light-independent. Introduction of mouse melanopsin restored normal thermotactic behavior in ninaE mutant larvae. We propose that rhodopsins represent a class of evolutionarily conserved GPCRs that are required for initiating thermosensory signaling cascades.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Eye Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, G-Protein-Coupled,
http://linkedlifedata.com/resource/pubmed/chemical/Rhodopsin,
http://linkedlifedata.com/resource/pubmed/chemical/Rod Opsins,
http://linkedlifedata.com/resource/pubmed/chemical/TRPC Cation Channels,
http://linkedlifedata.com/resource/pubmed/chemical/TrpA1 protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/melanopsin,
http://linkedlifedata.com/resource/pubmed/chemical/ninaE protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
11
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pubmed:volume |
331
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1333-6
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pubmed:meshHeading |
pubmed-meshheading:21393546-Animals,
pubmed-meshheading:21393546-Drosophila Proteins,
pubmed-meshheading:21393546-Drosophila melanogaster,
pubmed-meshheading:21393546-Eye Proteins,
pubmed-meshheading:21393546-Larva,
pubmed-meshheading:21393546-Light,
pubmed-meshheading:21393546-Mice,
pubmed-meshheading:21393546-Movement,
pubmed-meshheading:21393546-Mutation,
pubmed-meshheading:21393546-Photoreceptor Cells, Invertebrate,
pubmed-meshheading:21393546-Receptors, G-Protein-Coupled,
pubmed-meshheading:21393546-Rhodopsin,
pubmed-meshheading:21393546-Rod Opsins,
pubmed-meshheading:21393546-Signal Transduction,
pubmed-meshheading:21393546-TRPC Cation Channels,
pubmed-meshheading:21393546-Temperature,
pubmed-meshheading:21393546-Thermosensing
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pubmed:year |
2011
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pubmed:articleTitle |
Function of rhodopsin in temperature discrimination in Drosophila.
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pubmed:affiliation |
Department of Biological Chemistry, Center for Sensory Biology, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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