Abstract

Recent studies suggest that the fly uses the inositol lipid signaling system for visual excitation and that the Drosophila transient receptor potential (trp) mutation disrupts this process subsequent to the production of IP3. In this paper, we show that trp encodes a novel 1275 amino acid protein with eight putative transmembrane segments. Immunolocalization indicates that the trp protein is expressed predominantly in the rhabdomeric membranes of the photoreceptor cells.

Keywords

Visual phototransductionTransient receptor potential channelTransmembrane proteinBiologyDrosophila melanogasterCell biologyTransmembrane domainDrosophilidaeLocus (genetics)Signal transductionMutantRhodopsinGeneBiochemistryReceptorRetinal

MeSH Terms

Amino Acid SequenceAnimalsBase SequenceCalcium ChannelsDNADrosophila ProteinsDrosophila melanogasterGenesInositol PhosphatesInsect HormonesInsect ProteinsMembrane ProteinsMolecular Sequence DataPhotoreceptor CellsProtein ConformationSignal TransductionTransient Receptor Potential Channels

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Publication Info

Year
1989
Type
article
Volume
2
Issue
4
Pages
1313-1323
Citations
1119
Access
Closed

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1119
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Cite This

Craig Montell, Gerald M. Rubin (1989). Molecular characterization of the drosophila trp locus: A putative integral membrane protein required for phototransduction. Neuron , 2 (4) , 1313-1323. https://doi.org/10.1016/0896-6273(89)90069-x

Identifiers

DOI
10.1016/0896-6273(89)90069-x
PMID
2516726

Data Quality

Data completeness: 81%