rdf:type |
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lifeskim:mentions |
umls-concept:C0013138,
umls-concept:C0023764,
umls-concept:C0205396,
umls-concept:C0312422,
umls-concept:C0376451,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1704259,
umls-concept:C1705987
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pubmed:issue |
10
|
pubmed:dateCreated |
2004-9-28
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pubmed:abstractText |
The rolling blackout (rbo) gene encodes an integral plasma membrane lipase required for Drosophila phototransduction. Photoreceptors are enriched for the RBO protein, and temperature-sensitive rbo mutants show reversible elimination of phototransduction within minutes, demonstrating an acute requirement for the protein. The block is activity dependent, indicating that the action of RBO is use dependent. Conditional rbo mutants show activity-dependent depletion of diacylglycerol and concomitant accumulation of phosphatidylinositol phosphate and phosphatidylinositol 4,5-bisphosphate within minutes of induction, suggesting rapid downregulation of phospholipase C (PLC) activity. The RBO requirement identifies an essential regulatory step in G-protein-coupled, PLC-dependent inositol lipid signaling mediating activation of TRP and TRPL channels during phototransduction.
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pubmed:grant |
|
pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carboxylic Ester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Diglycerides,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 4,5-Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases,
http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1097-6256
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1070-8
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:15361878-Amino Acid Sequence,
pubmed-meshheading:15361878-Animals,
pubmed-meshheading:15361878-Animals, Genetically Modified,
pubmed-meshheading:15361878-Base Sequence,
pubmed-meshheading:15361878-Carboxylic Ester Hydrolases,
pubmed-meshheading:15361878-Cell Membrane,
pubmed-meshheading:15361878-Chromosome Mapping,
pubmed-meshheading:15361878-DNA, Complementary,
pubmed-meshheading:15361878-Diglycerides,
pubmed-meshheading:15361878-Down-Regulation,
pubmed-meshheading:15361878-Drosophila Proteins,
pubmed-meshheading:15361878-Drosophila melanogaster,
pubmed-meshheading:15361878-GTP-Binding Proteins,
pubmed-meshheading:15361878-Gene Expression Regulation,
pubmed-meshheading:15361878-Membrane Potentials,
pubmed-meshheading:15361878-Membrane Proteins,
pubmed-meshheading:15361878-Molecular Sequence Data,
pubmed-meshheading:15361878-Mutation,
pubmed-meshheading:15361878-Phosphatidylinositol 4,5-Diphosphate,
pubmed-meshheading:15361878-Phospholipases,
pubmed-meshheading:15361878-Photoreceptor Cells, Invertebrate,
pubmed-meshheading:15361878-Temperature,
pubmed-meshheading:15361878-Type C Phospholipases,
pubmed-meshheading:15361878-Vision, Ocular
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pubmed:year |
2004
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pubmed:articleTitle |
Rolling blackout, a newly identified PIP2-DAG pathway lipase required for Drosophila phototransduction.
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pubmed:affiliation |
Department of Biological Sciences, Vanderbilt Kennedy Center, Vanderbilt Brain Institute, Vanderbilt University, Nashville, Tennessee 37235-1634, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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