Phosrestin I undergoes the earliest light-induced phosphorylation by a calcium/calmodulin-dependent protein kinase in drosophila photoreceptors

Matsumoto, Hiroyuki; Kurien, Biji T.; Takagi, Yuichiro; Kahn, Esther S.; Kinumi, Tomoya; Komori, Naoka; Yamada, Teppei; Hayashi, Fumio; Isono, Kunio; Pak, William L.; Jackson, Kenneth W.; Tobin, Sara L.

doi:10.1016/0896-6273(94)90309-3

Cited by 110 publications

(69 citation statements)

References 53 publications

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“…Both of these steps are regulated by Ca 2+ /calmodulin (CaM). Arr2 is phosphorylated by Ca 2+ /CaM-dependent kinase II and this modification is required for dissociation of the rhodopsin/ Arr2 interaction [87,[102][103][104][105].…”

Section: The Rhodopsin Cycle In Drosophilamentioning

confidence: 99%

“…The converse of retinal degeneration resulting from too little endocytosis of rhodopsin is the cell death that occurs [103,105]. Mutations such as those in trp and norpA that prevent the normal rise in Ca 2+ after light stimulation result in stable Rh1/Arr2 complexes and retinal degeneration.…”

Section: Retinal Degenerationmentioning

confidence: 99%

“…Both the trp 14 and trp P343 phenotypes are suppressed by loss-of-function mutation in calx and by mutations in arr2 [150]. Thus, the loss of TRP channel function may lead to stable Rh1/Arr2 complexes, and this could result from a defect in CaM kinase II-dependent phosphorylation of Arr2, which is necessary for dissociation of Arr2 from Rh1 [103,105].…”

Section: Retinal Degenerationmentioning

confidence: 99%

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Phototransduction and retinal degeneration in Drosophila

Wang

Montell

2007

Pflugers Arch - Eur J Physiol

261

303

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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.

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Section: The Rhodopsin Cycle In Drosophilamentioning

confidence: 99%

Section: Retinal Degenerationmentioning

confidence: 99%

Section: Retinal Degenerationmentioning

confidence: 99%

See 1 more Smart Citation

Phototransduction and retinal degeneration in Drosophila

Wang

Montell

2007

Pflugers Arch - Eur J Physiol

261

303

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“…Metarhodopsin deactivation is achieved via phosphorylation by rhodopsin kinase ( Fig. 10; Bentrop and Paulsen, 1986;Doza et al, 1992;Byk et al, 1993) and binding of two types of arrestin molecules (Dolph et al, 1993); the arrestins are also called phosrestins, because they are rapidly phosphorylated after light onset (Matsumoto and Yamada, 1991;Matsumoto et al, 1994).…”

Section: Prolonged Depolarizing Afterpotentialmentioning

confidence: 99%

Insect retinal pigments: Spectral characteristics and physiological functions

Stavenga

1995

Progress in Retinal and Eye Research

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“…The dissociation of Arr2 from rhodopsin requires photoconversion of metarhodopsin back to rhodopsin, followed by dephosphorylation of rhodospsin by the Ca 2+ dependent protein phosphatase RDGC (retinat degeneration C) (Byk et al, 1993;Dolph et al, 1993;Steele et al, 1992;Yamada et al, 1990). Arr2 is phosphorylated by calcium/calmodulin-dependent kinase II (CamKII) (Matsumoto et al, 1994;Yamada et al, 1990), which is activated by Ca 2+ influx through the light activated TRP and TRPL channels (Alloway and Dolph, 1999;Byk et al, 1993;Kiselev et al, 2000;Peretz et al, 1994). Mutations which cause stable association between Arr2 and metarhodopsin result in clathrin-dependent endocytosis of the metarhodopsin-Arr2 complexes into the cell body that eventually lead to degeneration of the photoreceptor cell (Alloway and Dolph, 1999;Alloway et al, 2000;Kiselev et al, 2000;Orem and Dolph, 2002).…”

Section: Light Adaptation Through Phosphoinositide and Ninac Myosin Imentioning

confidence: 99%

Light-regulated translocation of signaling proteins in Drosophila photoreceptors

Frechter

Minke

2006

Journal of Physiology-Paris

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Illumination of Drosophila photoreceptor cells induces multi-facet responses, which include generation of the photoreceptor potential, screening pigment migration and translocation of signaling proteins which is the focus of recent extensive research. Translocation of three signaling molecules is covered in this review: (1) Light-dependent translocation of arrestin from the cytosol to the signaling membrane, the rhabdomere, determines the lifetime of activated rhodopsin. Arrestin translocates in PIP 3 and NINAC myosin III dependent manner, and specific mutations which disrupt the interaction between arrestin and PIP 3 or NINAC also impair the light-dependant translocation of arrestin and the termination of the response to light. (2) Activation of Drosophila visual G protein, DGq, causes a massive and reversible, translocation of the α subunit from the signaling membrane to the cytosol, accompanied by activity-dependent architectural changes. Analysis of the translocation and the recovery kinetics of DGq α in wild-type flies and specific visual mutants indicated that DGq α is necessary but not sufficient for the architectural changes. (3) The TRP-like (TRPL) but not TRP channels translocate in a light-dependent manner between the rhabdomere and the cell body. As a physiological consequence of this light-dependent modulation of the TRP/TRPL ratio, the photoreceptors of dark-adapted flies operate at a wider dynamic range, which allows the photoreceptors enriched with TRPL to function better in darkness and dim background illumination. Altogether, signal-dependent movement of signaling proteins plays a major role in the maintenance and function of photoreceptor cells.

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Phosrestin I undergoes the earliest light-induced phosphorylation by a calcium/calmodulin-dependent protein kinase in drosophila photoreceptors

Cited by 110 publications

References 53 publications

Phototransduction and retinal degeneration in Drosophila

Phototransduction and retinal degeneration in Drosophila

Insect retinal pigments: Spectral characteristics and physiological functions

Light-regulated translocation of signaling proteins in Drosophila photoreceptors

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