Diversity of visual pigments from the viewpoint of G protein activation—comparison with other G protein-coupled receptors

Shichida, Yoshinori; Yamashita, Takahiro

doi:10.1039/b300434a

Cited by 24 publications

(20 citation statements)

References 122 publications

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“…A small fraction of type II opsins also play roles in circadian rhythm and pigment regulation (Sakmar, 2002; Shichida and Yamashita, 2003). Type II opsins primarily function as G protein-coupled receptors (GPCRs) and appear to all use the 11- cis isomer of retinal (or derivatives) for photon absorption (Figure 2A, bottom).…”

Section: Fundamentalsmentioning

confidence: 99%

The Microbial Opsin Family of Optogenetic Tools

Zhang

Vierock

Yizhar

et al. 2011

Cell

483

467

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The capture and utilization of light is an exquisitely evolved process. The single-component microbial opsins, although more limited than multicomponent cascades in processing, display unparalleled compactness and speed. Recent advances in understanding microbial opsins have been driven by molecular engineering for optogenetics and by comparative genomics. Here we provide a Primer on these light-activated ion channels and pumps, describe a group of opsins bridging prior categories, and explore the convergence of molecular engineering and genomic discovery for the utilization and understanding of these remarkable molecular machines.

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Section: Fundamentalsmentioning

confidence: 99%

The Microbial Opsin Family of Optogenetic Tools

Zhang

Vierock

Yizhar

et al. 2011

Cell

483

467

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“…It is widely accepted that opsins have evolved from a non-light-sensing G protein-coupled receptor (GPCR) [2]. More than 2000 opsins have been identified in both vertebrates and invertebrates, and they are divided into several classes.…”

Section: Introductionmentioning

confidence: 99%

Beta-Arrestin Functionally Regulates the Non-Bleaching Pigment Parapinopsin in Lamprey Pineal

et al. 2011

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The light response of vertebrate visual cells is achieved by light-sensing proteins such as opsin-based pigments as well as signal transduction proteins, including visual arrestin. Previous studies have indicated that the pineal pigment parapinopsin has evolutionally and physiologically important characteristics. Parapinopsin is phylogenetically related to vertebrate visual pigments. However, unlike the photoproduct of the visual pigment rhodopsin, which is unstable, dissociating from its chromophore and bleaching, the parapinopsin photoproduct is stable and does not release its chromophore. Here, we investigated arrestin, which regulates parapinopsin signaling, in the lamprey pineal organ, where parapinopsin and rhodopsin are localized to distinct photoreceptor cells. We found that beta-arrestin, which binds to stimulated G protein-coupled receptors (GPCRs) other than opsin-based pigments, was localized to parapinopsin-containing cells. This result stands in contrast to the localization of visual arrestin in rhodopsin-containing cells. Beta-arrestin bound to cultured cell membranes containing parapinopsin light-dependently and translocated to the outer segments of pineal parapinopsin-containing cells, suggesting that beta-arrestin binds to parapinopsin to arrest parapinopsin signaling. Interestingly, beta-arrestin colocalized with parapinopsin in the granules of the parapinopsin-expressing cell bodies under light illumination. Because beta-arrestin, which is a mediator of clathrin-mediated GPCR internalization, also served as a mediator of parapinopsin internalization in cultured cells, these results suggest that the granules were generated light-dependently by beta-arrestin-mediated internalization of parapinopsins from the outer segments. Therefore, our findings imply that beta-arrestin-mediated internalization is responsible for eliminating the stable photoproduct and restoring cell conditions to the original dark state. Taken together with a previous finding that the bleaching pigment evolved from a non-bleaching pigment, vertebrate visual arrestin may have evolved from a “beta-like” arrestin by losing its clathrin-binding domain and its function as an internalization mediator. Such changes would have followed the evolution of vertebrate visual pigments, which generate unstable photoproducts that independently decay by chromophore dissociation.

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“…Although information about the parallel evolution of the many proteins that are involved in phototransduction is rapidly emerging 90,91 , the greatest progress to date has been made in relation to the opsin photopigments, on which we now concentrate. FIGURE 3 shows a phylogenetic tree of important visual and non-visual opsins 92 .…”

Section: The Evolution Of Vertebrate Opsinsmentioning

confidence: 99%

Evolution of the vertebrate eye: opsins, photoreceptors, retina and eye cup

2007

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Charles Darwin appreciated the conceptual difficulty in accepting that an organ as wonderful as the vertebrate eye could have evolved through natural selection. He reasoned that if appropriate gradations could be found that were useful to the animal and were inherited, then the apparent difficulty would be overcome. Here, we review a wide range of findings that capture glimpses of the gradations that appear to have occurred during eye evolution, and provide a scenario for the unseen steps that have led to the emergence of the vertebrate eye.

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Diversity of visual pigments from the viewpoint of G protein activation—comparison with other G protein-coupled receptors

Cited by 24 publications

References 122 publications

The Microbial Opsin Family of Optogenetic Tools

The Microbial Opsin Family of Optogenetic Tools

Beta-Arrestin Functionally Regulates the Non-Bleaching Pigment Parapinopsin in Lamprey Pineal

Evolution of the vertebrate eye: opsins, photoreceptors, retina and eye cup

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