Isolation of a putative phospholipase c gene of drosophila, norpA, and its role in phototransduction

Bloomquist, Brian T.; Shortridge, Randall D.; Schneuwly, Stephan; Perdew, M H; Montell, Craig; Steller, Hermann; Rubin, Gerald M.; Pak, William L.

doi:10.1016/s0092-8674(88)80017-5

Cited by 643 publications

(433 citation statements)

References 47 publications

Supporting

Mentioning

418

Contrasting

Unclassified

Order By: Relevance

“…6a) [5,91]. The critical role for NORPA for activation is illustrated by the observation that strong alleles of norpA, such as norpA P24 , abolish the photoresponse (Fig.…”

Section: G Q Protein In Phototransductionmentioning

confidence: 99%

“…These include the demonstration that the cascade operates through activation of a phospholipase Cβ (PLC) [5] and opening of the TRP and TRPL cation channels [6][7][8][9] (Fig. 1).…”

Section: Overview and Relationship Of Drosophila To Mammalian Phototrmentioning

confidence: 99%

“…After exchange of the guanosine diphosphate (GDP) bound to the Gα q for GTP, the Gα q and Gβγ subunits dissociate and the activated Gα q -GTP binds to the PLC encoded by norpA (no receptor potential A) [5,115]. The Gα q is critical for the photoresponse since the Gα q mutant (dG q 1 ) shows a 1,000-fold loss in light sensitivity [110].…”

Section: G Q Protein In Phototransductionmentioning

confidence: 99%

“…The critical role for NORPA for activation is illustrated by the observation that strong alleles of norpA, such as norpA P24 , abolish the photoresponse (Fig. 3b) [5]. Weak alleles result in decreases in light sensitivity and activation rates, which are linearly dependent on the levels of PLC activity [120,121].…”

Section: G Q Protein In Phototransductionmentioning

confidence: 99%

“…At least two different forms of PLCs are encoded by norpA, only one of which (subtype I) is primarily expressed in the retina [5,124,125]. As is typical of other phospholipase Cβ proteins, both NORPA isoforms have a membrane binding PH domain, a Ca 2+ interacting EF-hand, a divided phospholipase catalytic region consisting of X and Y core domains, and a putative Gα q binding C2 domain (Fig.…”

Section: G Q Protein In Phototransductionmentioning

confidence: 99%

See 4 more Smart Citations

Phototransduction and retinal degeneration in Drosophila

Wang

Montell

2007

Pflugers Arch - Eur J Physiol

261

303

View full text Add to dashboard Cite

Drosophila visual transduction is the fastest known G-protein-coupled signaling cascade and has therefore served as a genetically tractable animal model for characterizing rapid responses to sensory stimulation. Mutations in over 30 genes have been identified, which affect activation, adaptation, or termination of the photoresponse. Based on analyses of these genes, a model for phototransduction has emerged, which involves phosphoinoside signaling and culminates with opening of the TRP and TRPL cation channels. Many of the proteins that function in phototransduction are coupled to the PDZ containing scaffold protein INAD and form a supramolecular signaling complex, the signalplex. Arrestin, TRPL, and Gα q undergo dynamic light-dependent trafficking, and these movements function in long-term adaptation. Other proteins play important roles either in the formation or maturation of rhodopsin, or in regeneration of phosphatidylinositol 4,5-bisphosphate (PIP 2 ), which is required for the photoresponse. Mutation of nearly any gene that functions in the photoresponse results in retinal degeneration. The underlying bases of photoreceptor cell death are diverse and involve mechanisms such as excessive endocytosis of rhodopsin due to stable rhodopsin/arrestin complexes and abnormally low or high levels of Ca 2+ . Drosophila visual transduction appears to have particular relevance to the cascade in the intrinsically photosensitive retinal ganglion cells in mammals, as the photoresponse in these latter cells appears to operate through a remarkably similar mechanism.

show abstract

“…6a) [5,91]. The critical role for NORPA for activation is illustrated by the observation that strong alleles of norpA, such as norpA P24 , abolish the photoresponse (Fig.…”

Section: G Q Protein In Phototransductionmentioning

confidence: 99%

“…These include the demonstration that the cascade operates through activation of a phospholipase Cβ (PLC) [5] and opening of the TRP and TRPL cation channels [6][7][8][9] (Fig. 1).…”

Section: Overview and Relationship Of Drosophila To Mammalian Phototrmentioning

confidence: 99%

Section: G Q Protein In Phototransductionmentioning

confidence: 99%

Section: G Q Protein In Phototransductionmentioning

confidence: 99%

Section: G Q Protein In Phototransductionmentioning

confidence: 99%

See 3 more Smart Citations

Phototransduction and retinal degeneration in Drosophila

Wang

Montell

2007

Pflugers Arch - Eur J Physiol

261

303

View full text Add to dashboard Cite

show abstract

Immunolocalization of Drosophila eye‐specific diacylgylcerol kinase, rdgA , which is essential for the maintenance of the photoreceptor

et al. 1997

View full text Add to dashboard Cite

The Drosophila retinal degeneration A (rdgA) mutant has photoreceptor cells that degenerate within a week after eclosion. The degeneration starts with the disruption of the subrhabdomeric cisternae (SRC), which are the organelles essential for the transport of phospholipids to the photoreceptive membranes. Our previous biochemical and molecular studies suggested that the rdgA gene encodes an eye‐specific diacylglycerol kinase (DGK). In this study, we show that retinal degeneration is prevented by the introduction of the eye‐DGK gene in the rdgA mutant genome, suggesting that the DGK activity is crucial for the maintenance of the photoreceptor. Furthermore, by immunohistochemical analysis, we have demonstrated that the rdgA protein is predominantly associated with the SRC, suggesting that the conversion from diacylglycerol (DG) to phosphatidic acid (PA) most actively occurs in SRC. The analysis of the eyes of mutants homozygous for rdgA and eye‐protein kinase C mutations indicates that retinal degeneration is caused by the deficiency of PA rather than excessive accumulation of DG. From these data, we conclude that the production of PA in the SRC membranes is essential for the maintenance of the photoreceptor. © 1997 John Wiley & Sons, Inc. J Neurobiol 32: 695–706, 1997

show abstract

Modulation of the dihydropyridine‐sensitive calcium channels in Drosophila by a phospholipase C‐mediated pathway

Singh

1997

J. Neurobiol.

View full text Add to dashboard Cite

Disruption of phospholipase C‐β (PLC) by the norpA mutations of Drosophila renders flies blind by affecting the light‐evoked photoreceptor potential. We report here that the norpA‐coded PLC modulates the 1,4‐dihydropyridine (DHP)‐sensitive Ca2+ channels in larval muscles. The DHP‐sensitive current was reduced in the norpA mutants. Application of 1 μM phorbol 12‐myristate 13‐acetate (TPA) and 1 μM phorbol 12,13‐didecanoate (PDD), activators of protein kinase C (PKC), rescued the current in the mutant fibers without significantly affecting the normal current. 4α‐phorbol 12,13‐didecanoate (4αPDD), an inactive analog of PDD, did not affect either the normal or the mutant current. One micromolar bisindolylmaleimide (BIM), an inhibitor of PKC, reduced the current in the normal fibers without affecting the mutant current. 300 μM sn‐1,2‐dioctanoyl‐glycerol (DOG), an analog of diacylglycerol (DAG), increased the current in the mutant fibers. These experiments suggest that the DHP‐sensitive Ca2+ channels in Drosophila may be modulated by the PLC‐DAG‐PKC pathway, and that the same PLC isozyme which is involved in phototransduction in the adult flies may also modulate muscle Ca2+ channels in the larval stage of development. © 1997 John Wiley & Sons, Inc. J Neurobiol 33: 265–275, 1997

show abstract

Isolation of a putative phospholipase c gene of drosophila, norpA, and its role in phototransduction

Cited by 643 publications

References 47 publications

Phototransduction and retinal degeneration in Drosophila

Phototransduction and retinal degeneration in Drosophila

Immunolocalization of Drosophila eye‐specific diacylgylcerol kinase, rdgA , which is essential for the maintenance of the photoreceptor

Modulation of the dihydropyridine‐sensitive calcium channels in Drosophila by a phospholipase C‐mediated pathway

Contact Info

Product

Resources

About