UV-Sensitive Photoreceptor Protein OPN5 in Humans and Mice

Kojima, Daisuke; Mori, Suguru; Torii, Masaki; Wada, Akimori; Morishita, Rika; Fukada, Yoshitaka

doi:10.1371/journal.pone.0026388

Cited by 167 publications

(208 citation statements)

References 44 publications

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“…3). The photoresponsiveness of the Opn3 homolog-expressing cells incubated in the culture medium with 11-cis retinal was also higher than that of cells expressing the bleaching pigment bovine rhodopsin or another G i -coupled bistable pigment, Opn5 (10), suggesting that the Opn3 homologs might possess unknown molecular properties that provide an efficient decrease in cAMP in cultured cells, in addition to the bistable nature. Recently, neural activities have been successfully regulated by light through the introduction of light-sensing channels, namely the channelrhodopsins and their derivatives, establishing the field of optogenetics (31,32).…”

Section: Discussionmentioning

confidence: 98%

“…The G q -coupled opsin group is composed of the visual pigments from many invertebrates, such as insects and cephalopods, and the vertebrate opsin 4 (Opn4) homologs (melanopsins), which function as circadian photoreceptors in mammals (6). The scallop G o -coupled rhodopsin and amphioxus rhodopsin comprise the G o -coupled opsin group (7,8), and vertebrate opsin 5 (Opn5) was revealed to activate G i -type G proteins (9,10). In addition to these bilaterian opsins, we discovered a G s -coupled opsin in the visual cells of prebilaterian jellyfish (5).…”

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confidence: 99%

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Homologs of vertebrate Opn3 potentially serve as a light sensor in nonphotoreceptive tissue

Koyanagi

Takada

Nagata

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

150

214

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Most opsins selectively bind 11-cis retinal as a chromophore to form a photosensitive pigment, which underlies various physiological functions, such as vision and circadian photoentrainment. Recently, opsin 3 (Opn3), originally called encephalopsin or panopsin, and its homologs were identified in various tissues including brain, eye, and liver in both vertebrates and invertebrates, including human. Because Opn3s are mainly expressed in tissues that are not considered to contain sufficient amounts of 11-cis retinal to form pigments, the photopigment formation ability of Opn3 has been of interest. Here, we report the successful expression of Opn3 homologs, pufferfish teleost multiple tissue opsin (PufTMT) and mosquito Opn3 (MosOpn3) and show that these proteins formed functional photopigments with 11-cis and 9-cis retinals. The PufTMT-and MosOpn3-based pigments have absorption maxima in the blue-to-green region and exhibit a bistable nature. These Opn3 homolog-based pigments activate G i -type and G o -type G proteins light dependently, indicating that they potentially serve as light-sensitive G i /G o -coupled receptors. We also demonstrated that mammalian cultured cells transfected with the MosOpn3 or PufTMT became light sensitive without the addition of 11-cis retinal and the photosensitivity retained after the continuous light exposure, showing a reusable pigment formation with retinal endogenously contained in culture medium. Interestingly, we found that the MosOpn3 also acts as a light sensor when constituted with 13-cis retinal, a ubiquitously present retinal isomer. Our findings suggest that homologs of vertebrate Opn3 might function as photoreceptors in various tissues; furthermore, these Opn3s, particularly the mosquito homolog, could provide a promising optogenetic tool for regulating cAMP-related G protein-coupled receptor signalings.rhodopsin | phototransduction | nonvisual photoreception | opsin diversity M ost opsins bind 11-cis retinal as a chromophore to form a photosensitive pigment (opsin-based pigment) that serves as a light-sensitive G protein-coupled receptor (GPCR). The 11-cis to all-trans isomerization of the chromophore in an opsinbased pigment upon light absorption triggers G protein activation (1-4), and the photoreception of the opsin-based pigment initiates vision and nonvisual functions, including circadian entrainment and pupil responses. Several thousand opsins have been identified, and they are phylogenetically classified into eight groups based on the members that have existed early in animal evolution (5). The phylogenetic classification of each opsin also roughly corresponds to its molecular function. The G t -coupled opsin group contains vertebrate visual pigments, which activate transducin (G t )-type G proteins, and some nonvisual pigments, such as pinopsin, VA-opsin, parapinopsin, and parietopsin (1-4). The G q -coupled opsin group is composed of the visual pigments from many invertebrates, such as insects and cephalopods, and the vertebrate opsin 4 (Opn4) homologs (melanops...

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Section: Discussionmentioning

confidence: 98%

mentioning

confidence: 99%

Homologs of vertebrate Opn3 potentially serve as a light sensor in nonphotoreceptive tissue

Koyanagi

Takada

Nagata

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

150

214

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“…1). Protein extracts from mouse tissues were prepared as follows (8). Eight-week-old male mice were anesthetized and perfused with ice-cold PBS.…”

Section: Methodsmentioning

confidence: 99%

“…We also speculated from the complete conservation of the amino acid residues surrounding the chromophore between chicken and mammalian Opn5m proteins that mammalian Opn5m proteins should be UV-sensitive pigments, which was recently confirmed in mouse and human Opn5m proteins (8). In the present study, we compared the molecular properties of Opn5m proteins from zebrafish (fish), Xenopus tropicalis (amphibian), chicken (bird), mouse (mammal), and human (primate), paying particular attention to the differences between mammals and nonmammalian vertebrates.…”

mentioning

confidence: 87%

Evolution of Mammalian Opn5 as a Specialized UV-absorbing Pigment by a Single Amino Acid Mutation

Yamashita

Ono

Ohuchi

et al. 2014

Journal of Biological Chemistry

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Background: Opn5 is considered to regulate nonvisual photoreception in the retina and brain of animals. Results: Mouse and primate UV-sensitive Opn5 along with retinoid isomerase are localized in the preoptic hypothalamus. Conclusion: Mammalian Opn5 can function as a high sensitivity photosensor in the deep brain with the assistance of 11-cisretinal supplying system. Significance: Mammals, including humans, may detect short wavelength light within the brain via Opn5.

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“…RGR opsin was also shown to affect light-dependent mobilization of all-trans-retinyl esters (all-trans-REs) in mouse RPE cells (12). Neuropsin (OPN5) is a UV-sensitive bistable pigment also expressed in the vertebrate retina (13,14) that may play an additional role in photoentrainment (15,16).…”

mentioning

confidence: 99%

Peropsin modulates transit of vitamin A from retina to retinal pigment epithelium

Ng¹,

Lloyd²,

Eddington³

et al. 2017

Journal of Biological Chemistry

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Edited by Velia M. FowlerPeropsin is a non-visual opsin in both vertebrate and invertebrate species. In mammals, peropsin is present in the apical microvilli of retinal pigment epithelial (RPE) cells. These structures interdigitate with the outer segments of rod and cone photoreceptor cells. RPE cells play critical roles in the maintenance of photoreceptors, including the recycling of visual chromophore for the opsin visual pigments. Here, we sought to identify the function of peropsin in the mouse eye. To this end, we generated mice with a null mutation in the peropsin gene (Rrh). These mice exhibited normal retinal histology, normal morphology of outer segments and RPE cells, and no evidence of photoreceptor degeneration. Biochemically, Rrh ؊/؊ mice had ϳ2-fold higher vitamin A (all-trans-retinol (all-trans-ROL)) in the neural retina following a photobleach and 5-fold lower retinyl esters in the RPE. This phenotype was similar to those reported in mice that lack interphotoreceptor retinoid-binding protein (IRBP) or cellular retinol-binding protein, suggesting that peropsin plays a role in the movement of all-trans-ROL from photoreceptors to the RPE. We compared the phenotypes in mice lacking both peropsin and IRBP with those of mice lacking peropsin or IRBP alone and found that the retinoid phenotype was similarly severe in each of these knock-out mice. We conclude that peropsin controls all-trans-ROL movement from the retina to the RPE or may regulate all-trans-ROL storage within the RPE. We propose that peropsin affects light-dependent regulation of all-trans-ROL uptake from photoreceptors into RPE cells through an as yet undefined mechanism.

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UV-Sensitive Photoreceptor Protein OPN5 in Humans and Mice

Cited by 167 publications

References 44 publications

Homologs of vertebrate Opn3 potentially serve as a light sensor in nonphotoreceptive tissue

Homologs of vertebrate Opn3 potentially serve as a light sensor in nonphotoreceptive tissue

Evolution of Mammalian Opn5 as a Specialized UV-absorbing Pigment by a Single Amino Acid Mutation

Peropsin modulates transit of vitamin A from retina to retinal pigment epithelium

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