Opn5 is a UV-sensitive bistable pigment that couples with Gi subtype of G protein

Yamashita, Takahiro; Ohuchi, Hideyo; Tomonari, Sayuri; Ikeda, Keiko; Sakai, Kazumi; Shichida, Yoshinori

doi:10.1073/pnas.1012498107

Cited by 172 publications

(206 citation statements)

References 45 publications

(46 reference statements)

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“…As already reported, chicken Opn5m is a UVsensitive bistable pigment that forms 11-cis-and all-trans-retinal bound states, the latter of which activates the G i type of G protein (7). We also found that, although the apoprotein of Opn5m protein is extremely unstable, we could successfully obtain adequate amounts of chicken Opn5m pigment by adding 11-cis-or all-trans-retinal to the culture medium during the protein expression.…”

Section: Resultssupporting

confidence: 55%

“…The sample was irradiated with UV light through a UV-D35 glass filter (Asahi Technoglass), with yellow light through a Y-52 cutoff filter (Toshiba) or with orange light through an O-57 cutoff filter (Toshiba) from a 1 kW halogen lamp (Master HILUX-HR; Rikagaku). The absorption spectra of visible and UV light-absorbing forms of Opn5m proteins were calculated using the methods previously described (7). Briefly, the spectral region at wavelengths longer than the maximum of the main peak of the spectrum difference between the visible and UV light-absorbing forms of the pigment was best fitted with a template spectrum previously described (12,13).…”

Section: Methodsmentioning

confidence: 99%

“…In our previous reports, we succeeded in the purification of recombinant Opn5 proteins obtained by the expression of chicken Opn5 genes and reported that these proteins are UVsensitive bistable pigments that activate the G i type of G protein (4,7). 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).…”

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confidence: 99%

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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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Section: Resultssupporting

confidence: 55%

Section: Methodsmentioning

confidence: 99%

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confidence: 99%

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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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“…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%

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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“…2,8,25,26 A vertebrate nonvisual pigment, parapinopsin, shows bistable characteristics, although the pigment is classified into the Gt-coupled opsin group, which contains vertebrate visual pigments with 'bleaching property' (the photoproduct of vertebrate visual pigments releases its retinal chromophore and bleaches; Figure 1(c)). 27,28 A cnidarian opsin-based pigment (the jellyfish pigment) is converted to a stable photoproduct that does not revert to its original dark state by subsequent light irradiation, unlike typical bistable pigments.…”

Section: The Evolution Of Vertebrate Visual Pigments Pigment Propertiesmentioning

confidence: 99%

Evolution and diversity of opsins

Terakita

Kawano‐Yamashita

Koyanagi

2011

WIREs Membr Transp Signal

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Many animals capture light information via opsin-based pigments. Several thousands of opsins have been identified thus far and the opsin family is divided into eight groups. Members belonging to four out of the eight groups have been elucidated to couple to transducin, Go, Gs, and Gq, respectively, in photoreceptor cells. Accumulated evidence suggests a novel classification of the animal phototransductions, cyclic nucleotide signaling mediated by transducin, Go or Gs in ciliary photoreceptor cells and phosphoinositol signaling mediated by Gq in rhabdomeric photoreceptor cells. Varied opsin-based pigments are spectroscopically classified into two types, bleaching and bistable pigments; that is, the photoproduct of vertebrate visual pigments dissociates its chromophore retinal over time and bleaches, whereas most other opsin-based pigments convert to a stable photoproduct, which can revert to original dark state by subsequent light absorption. Mutational analyses of the both types of pigments implied that during molecular evolution of the vertebrae visual pigments, displacement of the counterion, important amino acid residue for visible light absorption of opsin-based pigment, resulted in not only unique bleaching property but also acquisition of red-sensitive visual pigment and higher G-protein activation ability generated by larger light-induced conformational change of the pigment. Interestingly, a bleaching pigment rhodopsin and parapinopsin, which closely relates to the vertebrate visual pigment but has a bistable nature, couple to visual arrestin and β arrestin, respectively, in the lamprey pineal organ, suggesting the bleaching property also might facilitate the evolution of visual arrestin which is specialized for vertebrate visual function. 

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Opn5 is a UV-sensitive bistable pigment that couples with Gi subtype of G protein

Cited by 172 publications

References 45 publications

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

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

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

Evolution and diversity of opsins

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