Loss of the phospholipase C gene product induces massive endocytosis of rhodopsin and arrestin in Drosophila photoreceptors

Orem, Nicholas R.; Dolph, Patrick J.

doi:10.1016/s0042-6989(01)00229-2

Cited by 34 publications

(29 citation statements)

References 41 publications

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“…Because of the lack of a receptor potential in norpA mutants, there is no rise in intra- cellular Ca 2ϩ levels (Peretz et al, 1994). The failure to activate Ca 2ϩ -dependent enzymes required for rhodopsin recycling causes excessive endocytosis of rhodopsin (Orem and Dolph, 2002), which is thought to initiate the cell death process (Alloway et al, 2000;Kiselev et al, 2000). We show here, in confirmation of a previous report (Alloway et al, 2000), that norpA degeneration is accompanied by morphological changes consistent with PCD processes, such as loss of cell contact, cytoplasmic condensation, and engulfment of the dying cells (Arends and Wyllie, 1991).…”

Section: Discussionmentioning

confidence: 99%

Limited Role of Developmental Programmed Cell Death Pathways inDrosophila norpARetinal Degeneration

Hsu¹,

Whaley²,

Frazer³

et al. 2004

J. Neurosci.

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We examined the role of programmed cell death (PCD) pathways in retinal degeneration caused by a mutation in the norpA gene. norpA degeneration shows morphological hallmarks of programmed cell death, specifically cytoplasmic condensation and engulfment of the dying photoreceptor cells by neighboring retinal pigment cells. However, genetic mosaic analysis of adult photoreceptors lacking rpr, hid, and grim show that these PCD inducers are not required for norpA degeneration. We showed previously that ectopic expression of either rpr or hid triggers rapid PCD in adult photoreceptors, and this is completely suppressed by the coexpression of the baculoviral P35 caspase inhibitor. In contrast, expression of P35 does not suppress norpA retinal degeneration, although a small delay in the rate of degeneration is observed in low light-low temperature conditions. P35 does not alter the morphological characteristics of norpA cell death. Overexpression of the Drosophila inhibitor of apoptosis Diap1 or a dominant-negative form of the Dronc caspase, even when coexpressed with P35, does not dramatically alter the time course of norpA degeneration. These results establish that the pathways responsible for PCD in development do not play a major role in adult retinal degeneration caused by norpA.

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Section: Discussionmentioning

confidence: 99%

Limited Role of Developmental Programmed Cell Death Pathways inDrosophila norpARetinal Degeneration

Hsu¹,

Whaley²,

Frazer³

et al. 2004

J. Neurosci.

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“…113 Based on these findings, it has been proposed that formation of a stable Rh1/Arr2 complex, and its internalization triggers retinal cell death. 56,113,125 …”

Section: Role Of Programmed Cell Deathmentioning

confidence: 99%

Molecular genetics of retinal degeneration: A Drosophila perspective

Shieh

2011

fly

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“…Because vertebrate transducin displays lightdependent translocation to detergent-resistant lipid rafts (Nair et al, 2002), it is possible that Gqα translocation involves a membrane-associated type of transport, such as endocytosis. Previous studies have suggested that endocytosis mediates the movement of rhodopsin-arrestin complexes from the rhabdomeres to the cell body in the retinal degeneration mutant rdgC (Kiselev et al, 2000) and in norpA mutants (Alloway et al, 2000;Orem and Dolph, 2002). To test whether translocation of Gqα occurs through endocytosis, we used the temperature-sensitive shibere mutant shi ts1 .…”

Section: Translocation Of Gqα Is Not Regulated By Shiberemediated Endmentioning

confidence: 99%

Light-dependent subcellular translocation of Gqα in Drosophila photoreceptors is facilitated by the photoreceptor-specific myosin III NINAC

Cronin

Diao

Tsunoda

2004

Journal of Cell Science

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We examine the light-dependent subcellular translocation of the visual Gqα protein between the signaling compartment, the rhabdomere and the cell body in Drosophila photoreceptors. We characterize the translocation of Gqα and provide the first evidence implicating the involvement of the photoreceptor-specific myosin III NINAC in Gqα transport. Translocation of Gqα from the rhabdomere to the cell body is rapid, taking less than 5 minutes. Higher light intensities increased the quantity of Gqα translocated out of the rhabdomeres from 20% to 75%, consistent with a mechanism for light adaptation. We demonstrate that translocation of Gqα requires rhodopsin, but none of the known downstream phototransduction components, suggesting that the signaling pathway triggering translocation occurs upstream of Gqα. Finally, we show that ninaC mutants display a significantly reduced rate of Gqα transport from the cell body to the rhabdomere, suggesting that NINAC might function as a light-dependent plus-end motor involved in the transport of Gqα.

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Loss of the phospholipase C gene product induces massive endocytosis of rhodopsin and arrestin in Drosophila photoreceptors

Cited by 34 publications

References 41 publications

Limited Role of Developmental Programmed Cell Death Pathways inDrosophila norpARetinal Degeneration

Limited Role of Developmental Programmed Cell Death Pathways inDrosophila norpARetinal Degeneration

Molecular genetics of retinal degeneration: A Drosophila perspective

Light-dependent subcellular translocation of Gqα in Drosophila photoreceptors is facilitated by the photoreceptor-specific myosin III NINAC

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