Source:http://linkedlifedata.com/resource/pubmed/id/16513351
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
2006-4-3
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pubmed:abstractText |
The Drosophila phototransduction cascade serves as a paradigm for characterizing the regulation of sensory signaling and TRP channels in vivo . Activation of these channels requires phospholipase C (PLC) and may depend on subsequent production of diacylglycerol (DAG) and downstream metabolites . DAG could potentially be produced through a second pathway involving the combined activities of a phospholipase D (PLD) and a phosphatidic acid (PA) phosphatase (PAP). However, a role for a PAP in the regulation of TRP channels has not been described. Here, we report the identification of a PAP, referred to as Lazaro (Laza). Mutations in laza caused a reduction in the light response and faster termination kinetics. Loss of laza suppressed the severity of the phenotype caused by mutation of the DAG kinase, RDGA , indicating that Laza functions in opposition to RDGA. We also showed that the retinal degeneration resulting from overexpression of the PLD was suppressed by elimination of Laza. These data demonstrate a requirement for a PLD/PAP-dependent pathway for achieving the maximal light response. The genetic interactions with both rdgA and Pld indicate that Laza functions in the convergence of both PLC- and PLD-coupled signaling in vivo.
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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/Diacylglycerol Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipase D,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Monoester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/lazaro protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0960-9822
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
4
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
723-9
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:16513351-Animals,
pubmed-meshheading:16513351-Diacylglycerol Kinase,
pubmed-meshheading:16513351-Drosophila,
pubmed-meshheading:16513351-Drosophila Proteins,
pubmed-meshheading:16513351-Kinetics,
pubmed-meshheading:16513351-Light,
pubmed-meshheading:16513351-Microscopy, Electron, Transmission,
pubmed-meshheading:16513351-Mutation,
pubmed-meshheading:16513351-Phosphatidylinositols,
pubmed-meshheading:16513351-Phospholipase D,
pubmed-meshheading:16513351-Phosphoric Monoester Hydrolases,
pubmed-meshheading:16513351-Retina,
pubmed-meshheading:16513351-Vision, Ocular
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pubmed:year |
2006
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pubmed:articleTitle |
Dependence on the Lazaro phosphatidic acid phosphatase for the maximum light response.
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pubmed:affiliation |
Department of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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