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

TitleDependence on the Lazaro phosphatidic acid phosphatase for the maximum light response
Publication TypeJournal Article
Year of Publication2006
AuthorsKwon Y, Montell C
JournalCurr Biol
Volume16
Pagination723-9
Date Published2006 Apr 4
ISSN0960-9822
KeywordsAnimals, Diacylglycerol Kinase, Drosophila, Drosophila Proteins, Kinetics, Light, Microscopy, Electron, Transmission, Mutation, Phosphatidylinositols, Phospholipase D, Phosphoric Monoester Hydrolases, Retina, Vision, Ocular
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.

DOI10.1016/j.cub.2006.02.057
Alternate JournalCurr. Biol.
PubMed ID16513351
Grant ListEY08117 / EY / NEI NIH HHS / United States
EY10852 / EY / NEI NIH HHS / United States