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PMID: 16513351 Published · ppublish English Journal Article Research Support, N.I.H., Extramural

Dependence on the Lazaro phosphatidic acid phosphatase for the maximum light response.

Current biology : CB ·Vol. 16 ·No. 7 ·2006-04-04 ·Pages 723-9

Kwon Y, Montell C

Abstract

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.

MeSH Terms
Animals Diacylglycerol Kinase/metabolism Drosophila/enzymology,genetics,physiology Drosophila Proteins/genetics,metabolism,physiology Kinetics Light Microscopy, Electron, Transmission Mutation Phosphatidylinositols/metabolism Phospholipase D/genetics,metabolism Phosphoric Monoester Hydrolases/genetics,metabolism,physiology Retina/metabolism,ultrastructure Vision, Ocular/physiology
Chemicals
Drosophila Proteins Phosphatidylinositols Diacylglycerol Kinase RdgA protein, Drosophila laza protein, Drosophila Phosphoric Monoester Hydrolases Phospholipase D
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Kwon Young
Department of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
Montell Craig
Article Info
Journal
Current biology : CB
Abbr.
Curr Biol
ISSN
0960-9822
Published
2006-04-04
Epub
2006-00-02
Pages
723-9
Language
English
Region
England
NLM ID
9107782
Subset
IM
Grants
NEI NIH HHS · EY08117 · United States
NEI NIH HHS · EY10852 · United States
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