Regulation of Arrestin Translocation by Ca2+ and Myosin III in Drosophila Photoreceptors

Hardie, Roger C.; Satoh, Akiko; Liu, Che-Hsiung

doi:10.1523/jneurosci.0924-12.2012

Cited by 7 publications

(10 citation statements)

References 38 publications

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“…Dissociated ommatidia were obtained by mechanical trituration and imaged using a 406 oil immersion objective and a Scion Firewire camera on an inverted Nikon microscope as previously described (e.g. Hardie et al, 2012). The standard bath solution contained (in mM) 120 NaCl, 5 KCl, 1.5 CaCl 2 , 4 MgCl 2 , 5 alanine, 20 proline, 10 N-Tris-(hydroxymethyl)-methyl-2-amino-ethanesulphonic acid (TES), pH 7.15.…”

Section: Gfp Imagingmentioning

confidence: 99%

Depletion of PtdIns(4,5)P2 underlies retinal degeneration in Drosophila trp mutants

Sengupta

Barber

Xia

et al. 2013

Journal of Cell Science

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SummaryThe prototypical transient receptor potential (TRP) channel is the major light-sensitive, and Ca 2+ -permeable channel in the microvillar photoreceptors of Drosophila. TRP channels are activated following hydrolysis of phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P 2 ] by the key effector enzyme phospholipase C (PLC). Mutants lacking TRP channels undergo light-dependent retinal degeneration, as a consequence of the reduced Ca 2+ influx. It has been proposed that degeneration is caused by defects in the Ca 2+ -dependent visual pigment cycle, which result in accumulation of toxic phosphorylated metarhodopsin-arrestin complexes (M PP -Arr2). Here we show that two interventions, which prevent accumulation of M PP -Arr2, namely rearing under red light or eliminating the C-terminal rhodopsin phosphorylation sites, failed to rescue degeneration in trp mutants. Instead, degeneration in trp mutants reared under red light was rescued by mutation of PLC. Degeneration correlated closely with the light-induced depletion of PtdIns(4,5)P 2 that occurs in trp mutants due to failure of Ca 2+ -dependent inhibition of PLC. Severe retinal degeneration was also induced in the dark in otherwise wild-type flies by overexpression of a bacterial PtdInsP n phosphatase (SigD) to deplete PtdIns(4,5)P 2 . In degenerating trp photoreceptors, phosphorylated Moesin, a PtdIns(4,5)P 2 -regulated membrane-cytoskeleton linker essential for normal microvillar morphology, was found to delocalize from the rhabdomere and there was extensive microvillar actin depolymerisation. The results suggest that compromised light-induced Ca 2+ influx, due to loss of TRP channels, leads to PtdIns(4,5)P 2 depletion, resulting in dephosphorylation of Moesin, actin depolymerisation and disintegration of photoreceptor structure.

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Section: Gfp Imagingmentioning

confidence: 99%

Depletion of PtdIns(4,5)P2 underlies retinal degeneration in Drosophila trp mutants

Sengupta

Barber

Xia

et al. 2013

Journal of Cell Science

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“…The smallest LICs, namely quantum bumps (Wu and Pak, 1975 ), result from single photon absorptions and the opening of ~15 TRP and TRPL channels, producing peak responses of ~10 pA (Henderson et al, 2000 ). The influx of Ca 2+ is particularly important, as it is not only the predominant mediator of the LIC but also a necessary modulator of the whole phototransduction machinery (Hardie, 1991 , 1995a ; Henderson et al, 2000 ; Hardie et al, 2001 , 2012 ; Gu et al, 2005 ; Liu et al, 2008 ).…”

Section: Introductionmentioning

confidence: 99%

Elementary and macroscopic light-induced currents and their Ca2+-dependence in the photoreceptors of Periplaneta americana

Immonen

Krause

et al. 2014

Front. Physiol.

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In a microvillar photoreceptor, absorption of an incident photon initiates a phototransduction reaction that generates a depolarizing light-induced current (LIC) in the microvillus. Although in-depth knowledge about these processes in photoreceptors of the fruitfly Drosophila is available, not much is known about their nature in other insect species. Here, we present description of some basic properties of both elementary and macroscopic LICs and their Ca2+-dependence in the photoreceptors of a dark-active species, the cockroach Periplaneta americana. Cockroach photoreceptors respond to single photon absorptions by generating quantum bumps with about 5-fold larger amplitudes than in Drosophila. At the macroscopic current level, cockroach photoreceptors responded to light with variable sensitivity and current waveform. This variability could be partially attributed to differences in whole-cell capacitance. Transient LICs, both elementary and macroscopic, showed only moderate dependence on extracellular Ca2+. However, with long light pulses, response inactivation was largely abolished and the overall size of LICs increased when extracellular Ca2+ was omitted. Finally, by determining relative ionic permeabilities from reversals of LICs, we demonstrate that when compared to Drosophila, cockroach light-gated channels are only moderately Ca2+-selective.

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“…Our finding that arrestin 2 becomes biotinylated only after rhodopsin is activated by light argues against unspecific biotinylation of rhabdomeral proteins, because the generation of Biotin-5ʹ-AMP by TurboID should be light-independent. It should be noted, however, that a significant fraction of arrestin 2 is translocated from the cell body to the rhabdomere upon illumination, thus enhancing the amount of arrestin 2 in the rhabdomere 35 , 36 . Attaching TurboID to an immobilized rhabdomeral protein such as NinaC, which is bound to the microvillar actin cytoskeleton, may help to distinguish between these alternatives.…”

Section: Resultsmentioning

confidence: 99%

In vivo identification of Drosophila rhodopsin interaction partners by biotin proximity labeling

Feizy,

Leuchtenberg,

Steiner

et al. 2024

Sci Rep

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Proteins exert their function through protein–protein interactions. In Drosophila, G protein-coupled receptors like rhodopsin (Rh1) interact with a G protein to activate visual signal transduction and with arrestins to terminate activation. Also, membrane proteins like Rh1 engage in protein–protein interactions during folding within the endoplasmic reticulum, during their vesicular transport and upon removal from the cell surface and degradation. Here, we expressed a Rh1-TurboID fusion protein (Rh1::TbID) in Drosophila photoreceptors to identify in vivo Rh1 interaction partners by biotin proximity labeling. We show that Rh1::TbID forms a functional rhodopsin that mediates biotinylation of arrestin 2 in conditions where arrestin 2 interacts with rhodopsin. We also observed biotinylation of Rh1::TbID and native Rh1 as well as of most visual signal transduction proteins. These findings indicate that the signaling components in the rhabdomere approach rhodopsin closely, within a range of ca. 10 nm. Furthermore, we have detected proteins engaged in the maturation of rhodopsin and elements responsible for the trafficking of membrane proteins, resembling potential interaction partners of Rh1. Among these are chaperons of the endoplasmic reticulum, proteins involved in Clathrin-mediated endocytosis as well as previously unnoticed contributors to rhodopsin transportation, such as Rab32, Vap33, or PIP82.

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Regulation of Arrestin Translocation by Ca2+ and Myosin III in Drosophila Photoreceptors

Cited by 7 publications

References 38 publications

Depletion of PtdIns(4,5)P2 underlies retinal degeneration in Drosophila trp mutants

Depletion of PtdIns(4,5)P2 underlies retinal degeneration in Drosophila trp mutants

Elementary and macroscopic light-induced currents and their Ca2+-dependence in the photoreceptors of Periplaneta americana

In vivo identification of Drosophila rhodopsin interaction partners by biotin proximity labeling

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