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Relevant bibliographies by topics / Visual opsin

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Academic literature on the topic 'Visual opsin'

Author: Grafiati

Published: 4 June 2021

Last updated: 16 February 2022

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Journal articles on the topic "Visual opsin"

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Kojima, Keiichi, Takahiro Yamashita, Yasushi Imamoto, Takehiro G. Kusakabe, Motoyuki Tsuda, and Yoshinori Shichida. "Evolutionary steps involving counterion displacement in a tunicate opsin." Proceedings of the National Academy of Sciences 114, no. 23 (May 22, 2017): 6028–33. http://dx.doi.org/10.1073/pnas.1701088114.

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Ci-opsin1 is a visible light-sensitive opsin present in the larval ocellus of an ascidian, Ciona intestinalis. This invertebrate opsin belongs to the vertebrate visual and nonvisual opsin groups in the opsin phylogenetic tree. Ci-opsin1 contains candidate counterions (glutamic acid residues) at positions 113 and 181; the former is a newly acquired position in the vertebrate visual opsin lineage, whereas the latter is an ancestral position widely conserved among invertebrate opsins. Here, we show that Glu113 and Glu181 in Ci-opsin1 act synergistically as counterions, which imparts molecular properties to Ci-opsin1 intermediate between those of vertebrate- and invertebrate-type opsins. Synergy between the counterions in Ci-opsin1 was demonstrated by E113Q and E181Q mutants that exhibit a pH-dependent spectral shift, whereas only the E113Q mutation in vertebrate rhodopsin yields this spectral shift. On absorbing light, Ci-opsin1 forms an equilibrium between two intermediates with protonated and deprotonated Schiff bases, namely the MI-like and MII-like intermediates, respectively. Adding G protein caused the equilibrium to shift toward the MI-like intermediate, indicating that Ci-opsin1 has a protonated Schiff base in its active state, like invertebrate-type opsins. Ci-opsin1’s G protein activation efficiency is between the efficiencies of vertebrate- and invertebrate-type opsins. Interestingly, the E113Y and E181S mutations change the molecular properties of Ci-opsin1 into those resembling invertebrate-type or bistable opsins and vertebrate ancient/vertebrate ancient-long or monostable opsins, respectively. These results strongly suggest that acquisition of counterion Glu113 changed the molecular properties of visual opsin in a vertebrate/tunicate common ancestor as a crucial step in the evolution of vertebrate visual opsins.

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Zhang, Tao, Li-Hui Cao, Sandeep Kumar, Nduka O. Enemchukwu, Ning Zhang, Alyssia Lambert, Xuchen Zhao, et al. "Dimerization of visual pigments in vivo." Proceedings of the National Academy of Sciences 113, no. 32 (July 26, 2016): 9093–98. http://dx.doi.org/10.1073/pnas.1609018113.

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It is a deeply engrained notion that the visual pigment rhodopsin signals light as a monomer, even though many G protein-coupled receptors are now known to exist and function as dimers. Nonetheless, recent studies (albeit all in vitro) have suggested that rhodopsin and its chromophore-free apoprotein, R-opsin, may indeed exist as a homodimer in rod disk membranes. Given the overwhelmingly strong historical context, the crucial remaining question, therefore, is whether pigment dimerization truly exists naturally and what function this dimerization may serve. We addressed this question in vivo with a unique mouse line (S-opsin+Lrat−/−) expressing, transgenically, short-wavelength–sensitive cone opsin (S-opsin) in rods and also lacking chromophore to exploit the fact that cone opsins, but not R-opsin, require chromophore for proper folding and trafficking to the photoreceptor’s outer segment. In R-opsin’s absence, S-opsin in these transgenic rods without chromophore was mislocalized; in R-opsin’s presence, however, S-opsin trafficked normally to the rod outer segment and produced functional S-pigment upon subsequent chromophore restoration. Introducing a competing R-opsin transmembrane helix H1 or helix H8 peptide, but not helix H4 or helix H5 peptide, into these transgenic rods caused mislocalization of R-opsin and S-opsin to the perinuclear endoplasmic reticulum. Importantly, a similar peptide-competition effect was observed even in WT rods. Our work provides convincing evidence for visual pigment dimerization in vivo under physiological conditions and for its role in pigment maturation and targeting. Our work raises new questions regarding a potential mechanistic role of dimerization in rhodopsin signaling.

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Upton, Brian A., Nicolás M. Díaz, Shannon A. Gordon, Russell N. Van Gelder, Ethan D. Buhr, and Richard A. Lang. "Evolutionary Constraint on Visual and Nonvisual Mammalian Opsins." Journal of Biological Rhythms 36, no. 2 (March 25, 2021): 109–26. http://dx.doi.org/10.1177/0748730421999870.

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Animals have evolved light-sensitive G protein–coupled receptors, known as opsins, to detect coherent and ambient light for visual and nonvisual functions. These opsins have evolved to satisfy the particular lighting niches of the organisms that express them. While many unique patterns of evolution have been identified in mammals for rod and cone opsins, far less is known about the atypical mammalian opsins. Using genomic data from over 400 mammalian species from 22 orders, unique patterns of evolution for each mammalian opsins were identified, including photoisomerases, RGR-opsin (RGR) and peropsin (RRH), as well as atypical opsins, encephalopsin (OPN3), melanopsin (OPN4), and neuropsin (OPN5). The results demonstrate that OPN5 and rhodopsin show extreme conservation across all mammalian lineages. The cone opsins, SWS1 and LWS, and the nonvisual opsins, OPN3 and RRH, demonstrate a moderate degree of sequence conservation relative to other opsins, with some instances of lineage-specific gene loss. Finally, the photoisomerase, RGR, and the best-studied atypical opsin, OPN4, have high sequence diversity within mammals. These conservation patterns are maintained in human populations. Importantly, all mammalian opsins retain key amino acid residues important for conjugation to retinal-based chromophores, permitting light sensitivity. These patterns of evolution are discussed along with known functions of each atypical opsin, such as in circadian or metabolic physiology, to provide insight into the observed patterns of evolutionary constraint.

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Liénard, Marjorie A., Gary D. Bernard, Andrew Allen, Jean-Marc Lassance, Siliang Song, Richard Rabideau Childers, Nanfang Yu, et al. "The evolution of red color vision is linked to coordinated rhodopsin tuning in lycaenid butterflies." Proceedings of the National Academy of Sciences 118, no. 6 (February 5, 2021): e2008986118. http://dx.doi.org/10.1073/pnas.2008986118.

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Color vision has evolved multiple times in both vertebrates and invertebrates and is largely determined by the number and variation in spectral sensitivities of distinct opsin subclasses. However, because of the difficulty of expressing long-wavelength (LW) invertebrate opsins in vitro, our understanding of the molecular basis of functional shifts in opsin spectral sensitivities has been biased toward research primarily in vertebrates. This has restricted our ability to address whether invertebrate Gq protein-coupled opsins function in a novel or convergent way compared to vertebrate Gt opsins. Here we develop a robust heterologous expression system to purify invertebrate rhodopsins, identify specific amino acid changes responsible for adaptive spectral tuning, and pinpoint how molecular variation in invertebrate opsins underlie wavelength sensitivity shifts that enhance visual perception. By combining functional and optophysiological approaches, we disentangle the relative contributions of lateral filtering pigments from red-shifted LW and blue short-wavelength opsins expressed in distinct photoreceptor cells of individual ommatidia. We use in situ hybridization to visualize six ommatidial classes in the compound eye of a lycaenid butterfly with a four-opsin visual system. We show experimentally that certain key tuning residues underlying green spectral shifts in blue opsin paralogs have evolved repeatedly among short-wavelength opsin lineages. Taken together, our results demonstrate the interplay between regulatory and adaptive evolution at multiple Gq opsin loci, as well as how coordinated spectral shifts in LW and blue opsins can act together to enhance insect spectral sensitivity at blue and red wavelengths for visual performance adaptation.

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PORTER, MEGAN L., MICHAEL J. BOK, PHYLLIS R. ROBINSON, and THOMAS W. CRONIN. "Molecular diversity of visual pigments in Stomatopoda (Crustacea)." Visual Neuroscience 26, no. 3 (May 2009): 255–65. http://dx.doi.org/10.1017/s0952523809090129.

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AbstractStomatopod crustaceans possess apposition compound eyes that contain more photoreceptor types than any other animal described. While the anatomy and physiology of this complexity have been studied for more than two decades, few studies have investigated the molecular aspects underlying the stomatopod visual complexity. Based on previous studies of the structure and function of the different types of photoreceptors, stomatopod retinas are hypothesized to contain up to 16 different visual pigments, with 6 of these having sensitivity to middle or long wavelengths of light. We investigated stomatopod middle- and long-wavelength-sensitive opsin genes from five species with the hypothesis that each species investigated would express up to six different opsin genes. In order to understand the evolution of this class of stomatopod opsins, we examined the complement of expressed transcripts in the retinas of species representing a broad taxonomic range (four families and three superfamilies). A total of 54 unique retinal opsins were isolated, resulting in 6–15 different expressed transcripts in each species. Phylogenetically, these transcripts form six distinct clades, grouping with other crustacean opsins and sister to insect long-wavelength visual pigments. Within these stomatopod opsin groups, intra- and interspecific clusters of highly similar transcripts suggest that there has been rampant recent gene duplication. Some of the observed molecular diversity is also due to ancient gene duplication events within the stem crustacean lineage. Using evolutionary trace analysis, 10 amino acid sites were identified as functionally divergent among the six stomatopod opsin clades. These sites form tight clusters in two regions of the opsin protein known to be functionally important: six in the chromophore-binding pocket and four at the cytoplasmic surface in loops II and III. These two clusters of sites indicate that stomatopod opsins have diverged with respect to both spectral tuning and signal transduction.

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Dalton, Brian E., Ellis R. Loew, Thomas W. Cronin, and Karen L. Carleton. "Spectral tuning by opsin coexpression in retinal regions that view different parts of the visual field." Proceedings of the Royal Society B: Biological Sciences 281, no. 1797 (December 22, 2014): 20141980. http://dx.doi.org/10.1098/rspb.2014.1980.

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Vision frequently mediates critical behaviours, and photoreceptors must respond to the light available to accomplish these tasks. Most photoreceptors are thought to contain a single visual pigment, an opsin protein bound to a chromophore, which together determine spectral sensitivity. Mechanisms of spectral tuning include altering the opsin, changing the chromophore and incorporating pre-receptor filtering. A few exceptions to the use of a single visual pigment have been documented in which a single mature photoreceptor coexpresses opsins that form spectrally distinct visual pigments, and in these exceptions the functional significance of coexpression is unclear. Here we document for the first time photoreceptors coexpressing spectrally distinct opsin genes in a manner that tunes sensitivity to the light environment. Photoreceptors of the cichlid fish, Metriaclima zebra , mix different pairs of opsins in retinal regions that view distinct backgrounds. The mixing of visual pigments increases absorbance of the corresponding background, potentially aiding the detection of dark objects. Thus, opsin coexpression may be a novel mechanism of spectral tuning that could be useful for detecting prey, predators and mates. However, our calculations show that coexpression of some opsins can hinder colour discrimination, creating a trade-off between visual functions.

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ISAYAMA, T., Y. CHEN, M. KONO, W. J. DEGRIP, J. X. MA, R. K. CROUCH, and C. L. MAKINO. "Differences in the pharmacological activation of visual opsins." Visual Neuroscience 23, no. 6 (November 2006): 899–908. http://dx.doi.org/10.1017/s0952523806230256.

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Opsins, like many other G-protein-coupled receptors, sustain constitutive activity in the absence of ligand. In partially bleached rods and cones, opsin's activity closes cGMP-gated channels and produces a state of “pigment adaptation” with reduced sensitivity to light and accelerated flash response kinetics. The truncated retinal analogue, β-ionone, further desensitizes partially bleached green-sensitive salamander rods, but enables partially bleached red-sensitive cones to recover dark-adapted physiology. Structural differences between rod and cone opsins were proposed to explain the effect. Rods and cones, however, also contain different transducins, raising the possibility that G-protein type determines the photoreceptor-specific effects of β-ionone. To test the two hypotheses, we applied β-ionone to partially bleached blue-sensitive rods and cones of salamander, two cells that couple the same cone-like opsin to either rod or cone transducin, respectively. Immunocytochemistry confirmed that all salamander rods contain one form of transducin, whereas all cones contain another. β-Ionone enhanced pigment adaptation in blue-sensitive rods, but it also did so in blue- and UV-sensitive cones. Furthermore, all recombinant salamander rod and cone opsins, with the exception of the red-sensitive cone opsin, activated rod transducin upon the addition of β-ionone. Thus opsin structure determines the identity of β-ionone as an agonist or an inverse agonist and in that respect distinguishes the red-sensitive cone opsin from all others.

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Musilova, Zuzana, Fabio Cortesi, Michael Matschiner, Wayne I. L. Davies, Jagdish Suresh Patel, Sara M. Stieb, Fanny de Busserolles, et al. "Vision using multiple distinct rod opsins in deep-sea fishes." Science 364, no. 6440 (May 9, 2019): 588–92. http://dx.doi.org/10.1126/science.aav4632.

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Vertebrate vision is accomplished through light-sensitive photopigments consisting of an opsin protein bound to a chromophore. In dim light, vertebrates generally rely on a single rod opsin [rhodopsin 1 (RH1)] for obtaining visual information. By inspecting 101 fish genomes, we found that three deep-sea teleost lineages have independently expanded their RH1 gene repertoires. Among these, the silver spinyfin (Diretmus argenteus) stands out as having the highest number of visual opsins in vertebrates (two cone opsins and 38 rod opsins). Spinyfins express up to 14 RH1s (including the most blueshifted rod photopigments known), which cover the range of the residual daylight as well as the bioluminescence spectrum present in the deep sea. Our findings present molecular and functional evidence for the recurrent evolution of multiple rod opsin–based vision in vertebrates.

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FASICK, JEFFRY I., THOMAS W. CRONIN, DAVID M. HUNT, and PHYLLIS R. ROBINSON. "The visual pigments of the bottlenose dolphin (Tursiops truncatus)." Visual Neuroscience 15, no. 4 (April 1998): 643–51. http://dx.doi.org/10.1017/s0952523898154056.

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To assess the dolphin's capacity for color vision and determine the absorption maxima of the dolphin visual pigments, we have cloned and expressed the dolphin opsin genes. On the basis of sequence homology with other mammalian opsins, a dolphin rod and long-wavelength sensitive (LWS) cone opsin cDNAs were identified. Both dolphin opsin cDNAs were expressed in mammalian COS-7 cells. The resulting proteins were reconstituted with the chromophore 11-cis-retinal resulting in functional pigments with absorption maxima (λmax) of 488 and 524 nm for the rod and cone pigments respectively. These λmax values are considerably blue shifted compared to those of many terrestrial mammals. Although the dolphin possesses a gene homologous to other mammalian short-wavelength sensitive (SWS) opsins, it is not expressed in vivo and has accumulated a number of deletions, including a frame-shift mutation at nucleotide position 31. The dolphin therefore lacks the common dichromatic form of color vision typical of most terrestrial mammals.

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VIHTELIC, THOMAS S., CHRISTOPHER J. DORO, and DAVID R. HYDE. "Cloning and characterization of six zebrafish photoreceptor opsin cDNAs and immunolocalization of their corresponding proteins." Visual Neuroscience 16, no. 3 (May 1999): 571–85. http://dx.doi.org/10.1017/s0952523899163168.

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Zebrafish (Danio rerio) represents an excellent genetic model for vertebrate visual system studies. Because the opsin proteins are ideal markers of specific photoreceptor cell types, we cloned six different zebrafish opsin cDNAs. Based on pairwise alignments and phylogenetic comparisons between the predicted zebrafish opsin amino acid sequences and other vertebrate opsins, the cDNAs encode rhodopsin, two different green opsins (zfgr1 and zfgr2), a red, a blue, and an ultraviolet opsin. Phylogenetic analysis indicates the zfgr1 protein occupies a well-resolved dendrogram branch separate from the other green opsins examined, while zebrafish ultraviolet opsin is closely related to the human blue- and chicken violet-sensitive proteins. Polyclonal antisera were generated against individual bacterial fusion proteins containing either the red, blue, or ultraviolet amino termini or the rod or green opsin carboxyl termini. Immunolocalization on adult zebrafish frozen sections demonstrates the green and red opsins are each expressed in different members of the double cone cell pair, the blue opsin is detected in long single cones, and the ultraviolet opsin protein is expressed in the short single cones. In 120-h postfertilization wholemounts, green, red, blue, and ultraviolet opsin-positive cells are detected in an orderly arrangement throughout the entire retina. The antibodies' photoreceptor-type specificity indicates they will be useful for characterizing both wild-type and mutant zebrafish retinas.

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Dissertations / Theses on the topic "Visual opsin"

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Hope, Andrew J. "Rod visual pigments of teleost fish." Thesis, University of Bristol, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.319236.

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Das, Debipriya. "Visual pigments, oil droplets and opsin sequences from the canary (Serinus canaria)." Thesis, University College London (University of London), 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.267989.

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Comar, William D. Ph D. "ESTABLISHING AND MANIPULATING THE DIMERIC INTERFACE OF VISUAL/NON-VISUAL OPSINS." University of Akron / OhioLINK, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=akron152882487417841.

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Martin, Gavin Jon. "A Molecular Phylogeny of Lampyridae with Insight into Visual and Bioluminescent Evolution." BYU ScholarsArchive, 2014. https://scholarsarchive.byu.edu/etd/5758.

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Fireflies are some of the most captivating organisms on the planet. Because of this, they have a rich history of study, especially concerning their bioluminescent and visual behavior. Among insects, opsin copy number variation has been shown to be quite diverse. However, within the beetles, very little work on opsins has been conducted. Here we look at the visual system of fireflies (Coleoptera: Lampyridae), which offer an elegant system in which to study visual evolution as it relates to their behavior and broader ecology. They are the best-known case of a terrestrial organism that communicates through the use bioluminescence. The molecular basis for this communication is relatively simple: one gene-family (opsins) controls the detection of the signal, and one gene family (luciferase) controls the production of the signal. We use a transcriptomic approach to sample for and investigate opsin evolution in fireflies. We also present the first total evidence approach using both an extensive molecular matrix and a robust morphological matrix to reconstruct the lampyrid phylogeny. We then use this phylogeny to assess the hypothesis that adult use of bioluminescence occurred after the origin of Lampyridae. We find evidence for only two expressed opsin classes in each of the nine firefly species studied, one in the ultra-violet sensitive and one in the long-wavelength sensitive areas of the visible spectrum. Despite the need for most adult fireflies to respond to a clearly sexual and colorful visual signal (bioluminescence) to maximize fitness, their visual system is relatively simple, and does not match the trend for opsin duplication found in other insect groups. All subfamilies except for Lampyrinae are recovered as monophyletic; Pterotinae and Ototretinae are recovered within the Lampyridae. The ancestral state of adult bioluminescence is suggested to be non-bioluminescent, with at least three gains and at least three losses.

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Lessios, Nicolas. "Using electroretinograms and multi-model inference to identify spectral classes of photoreceptors and relative opsin expression levels." PEERJ INC, 2017. http://hdl.handle.net/10150/625519.

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Understanding how individual photoreceptor cells factor in the spectral sensitivity of a visual system is essential to explain how they contribute to the visual ecology of the animal in question. Existing methods that model the absorption of visual pigments use templates which correspond closely to data from thin cross-sections of photoreceptor cells. However, few modeling approaches use a single framework to incorporate physical parameters of real photoreceptors, which can be fused, and can form vertical tiers. Akaike’s information criterion (AIC c ) was used here to select absorptance models of multiple classes of photoreceptor cells that maximize information, given visual system spectral sensitivity data obtained using extracellular electroretinograms and structural parameters obtained by histological methods. This framework was first used to select among alternative hypotheses of photoreceptor number. It identified spectral classes from a range of dark-adapted visual systems which have between one and four spectral photoreceptor classes. These were the velvet worm, Principapillatus hitoyensis , the branchiopod water flea, Daphnia magna , normal humans, and humans with enhanced S-cone syndrome, a condition in which S-cone frequency is increased due to mutations in a transcription factor that controls photoreceptor expression. Data from the Asian swallowtail, Papilio xuthus , which has at least five main spectral photoreceptor classes in its compound eyes, were included to illustrate potential effects of model over-simplification on multi-model inference. The multi-model framework was then used with parameters of spectral photoreceptor classes and the structural photoreceptor array kept constant. The goal was to map relative opsin expression to visual pigment concentration. It identified relative opsin expression differences for two populations of the bluefin killifish, Lucania goodei . The modeling approach presented here will be useful in selecting the most likely alternative hypotheses of opsin-based spectral photoreceptor classes, using relative opsin expression and extracellular electroretinography.

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Lagman, David. "Evolution of Vertebrate Vision by Means of Whole Genome Duplications : Zebrafish as a Model for Gene Specialisation." Doctoral thesis, Uppsala universitet, Institutionen för neurovetenskap, 2015. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-242781.

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The signalling cascade of rods and cones use different but related protein components. Rods and cones, emerged in the common ancestor of vertebrates around 500 million years ago around when two whole genome duplications took place, named 1R and 2R. These generated a large number of additional genes that could evolve new or more specialised functions. A third event, 3R, occurred in the ancestor of teleost fish. This thesis describes extensive phylogenetic and comparative synteny analyses of the opsins, transducin and phosphodiesterase (PDE6) of this cascade by including data from a wide selection of vertebrates. The expression of the zebrafish genes was also investigated. The results show that genes for these proteins duplicated in 1R and 2R as well as some in 3R. Expression analyses of the zebrafish genes revealed additional specialisations for the 3R gene duplicates. The transducin beta subunit genes, gnb1a and gnb1b, show co-localisation in rods but are expressed at different levels. Gnb3a and gnb3b show different expression in the adult retina with low expression of gnb3a and expression of gnb3b in cones of the dorso-medial retina. The transducin gamma subunit genes gngt2a and gngt2b are expressed in the ventral and dorso-medial retina respectively. The both of PDE6 gamma subunit genes, pde6ga and pde6gb are both expressed in rods but pde6ga shows rhythmic changes of expression with low daytime levels. Pde6ha and pde6hb are expressed in cones however pde6ha show high daytime expression. All investigated transducin and PDE6 subunit genes, but gnb1b, were also expressed in the adult pineal complex or at some point during development. These results provide compelling evidence that the 1R and 2R genome duplications facilitated the evolution of rods and cones by generating gene duplicates that could evolve distinct expression and function. This supports existence of colour vision before the origin of vertebrates, elaboration of this in the early vertebrate ancestor, along with origin of the black-and-white dim-light vision of rods. Furthermore, the different expression patterns observed in the zebrafish retina for teleost 3R duplicates demonstrate multiple additional specialisations.

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Hofmann, Lukas. "Structural Endeavors in the Retinoid (Visual) Cycle." Case Western Reserve University School of Graduate Studies / OhioLINK, 2017. http://rave.ohiolink.edu/etdc/view?acc_num=case1497045464455384.

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Katana, Radoslaw [Verfasser], Martin [Akademischer Betreuer] Göpfert, Martin [Gutachter] Göpfert, André [Gutachter] Fiala, Manuela [Gutachter] Schmidt, Gerd [Gutachter] Vorbrüggen, Jörg [Gutachter] Großhans, and Jan [Gutachter] Clemens. "Chromophore-independent roles of Drosophila opsin apoproteins and visual cycle components / Radoslaw Katana ; Gutachter: Martin Göpfert, André Fiala, Manuela Schmidt, Gerd Vorbrüggen, Jörg Großhans, Jan Clemens ; Betreuer: Martin Göpfert." Göttingen : Niedersächsische Staats- und Universitätsbibliothek Göttingen, 2019. http://d-nb.info/1178115844/34.

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Heath, Lesley Annette. "The molecular biology of avian visual pigments : evolution and spectral tuning." Thesis, University College London (University of London), 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.298706.

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Ocampo, Daza Daniel. "Evolution of Vertebrate Endocrine and Neuronal Gene Families : Focus on Pituitary and Retina." Doctoral thesis, Uppsala universitet, Farmakologi, 2013. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-191829.

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The duplication of genes followed by selection is perhaps the most prominent way in which molecular biological systems gain multiplicity, diversity and functional complexity in evolution. Whole genome duplications (WGDs) therefore have the potential of generating an extraordinary amount of evolutionary innovation. It is now accepted that the vertebrate lineage has gone through two rounds of WGD in its early stages, after the divergence of invertebrate chordates and before the emergence of jawed vertebrates. These basal vertebrate WGDs are called 2R for two rounds of whole genome duplication. An additional WGD called 3R occurred early in the evolution of teleost fishes, before the radiation of this species-rich group. This thesis describes the evolution of several endocrine and neuronal gene families in relation to the vertebrate WGDs, through a comparative genomic approach including both phylogenetic analyses and chromosomal location data across a wide range of vertebrate taxa. These results show that numerous endocrine gene families have expanded in 2R and in several cases also in 3R. These include the gene families of oxytocin and vasopressin receptors (OT/VP-R), somatostatin receptors (SSTR) and insulin-like growth factor binding proteins (IGFBP). For the OT/VP-R and SSTR families, previously undescribed subtypes were identified. The protein hormone family that includes growth hormone (GH), prolactin (PRL) and somatolactin (SL) acquired a new PRL gene in 2R, however the origins of GH, PRL and SL likely predate 2R. The corresponding family of receptors diversified during different time periods through a combination of local duplications and 3R. Neuronal gene families of the visual system have also expanded in 2R and 3R. The results presented here demonstrate that the vertebrate repertoire of visual opsin genes arose in 2R as part of chromosomal blocks that also include the OT/VP-R genes. The gene families including the transducin alpha, beta and gamma subunits also arose in 2R, hinting at the importance of these events in the diversification and specialization of phototransduction cascades for rods and cones. Thus, the whole genome duplications have been important contributors to the evolution of both vision and endocrine regulation in the vertebrates.

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Books on the topic "Visual opsin"

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Krzysztof, Palczewski, ed. Vertebrate phototransduction and the visual cycle. San Diego, CA: Academic Press, 2000.

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Vertebrate Phototransduction and the Visual Cycle, Part A, Volume 315 (Methods in Enzymology). Academic Press, 2000.

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Book chapters on the topic "Visual opsin"

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Kawamura, Shoji. "Evolutionary Diversification of Visual Opsin Genes in Fish and Primates." In From Genes to Animal Behavior, 329–49. Tokyo: Springer Japan, 2011. http://dx.doi.org/10.1007/978-4-431-53892-9_16.

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Kefalov, Vladimir J., M. Carter Cornwall, and Gordon L. Fain. "Physiological Studies of the Interaction Between Opsin and Chromophore in Rod and Cone Visual Pigments." In Methods in Molecular Biology, 95–114. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60327-325-1_5.

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Santillo, Silvia, Pierangelo Orlando, Luciano De Petrocellis, Luigia Cristino, Vittorio Guglielmotti, and Carlo Musio. "Molecular and Functional Diversity of Visual Pigments: Clues from the Photosensitive Opsin–Like Proteins of the Animal Model Hydra." In Brain, Vision, and Artificial Intelligence, 225–34. Berlin, Heidelberg: Springer Berlin Heidelberg, 2005. http://dx.doi.org/10.1007/11565123_23.

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Kojima, Daisuke, and Yoshitaka Fukada. "Non-Visual Photoreception by a Variety of Vertebrate Opsins." In Novartis Foundation Symposium 224 - Rhodopsins and Phototransduction, 265–90. Chichester, UK: John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470515693.ch15.

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Cronin, Thomas W., Sönke Johnsen, N. Justin Marshall, and Eric J. Warrant. "Visual Pigments and Photoreceptors." In Visual Ecology. Princeton University Press, 2014. http://dx.doi.org/10.23943/princeton/9780691151847.003.0003.

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This chapter focuses on visual pigments and photoreceptors. In living things, photoreception inevitably begins with a photochemical event—a molecule intercepts a photon of light and is somehow changed. Various molecules, generally known as photopigments, perform this function in animals and plants. The molecules involved in vision are called visual pigments. In all animals, vision ultimately depends on a single family of proteins that all have descended from one common ancestor—these are the opsins. The chapter cites the hydrothermal vent crab as a good example of how changes of visual pigments appearing in various developmental states reflect ecological adaptation. The animal's life stages require visual systems sampling opposite ends of the visual spectrum.

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"A Fish Eye Out of Water: Ten Visual Opsins in the Four-Eyed Fish, Anableps anableps." In Research Progress in Fisheries Science, 273–89. Apple Academic Press, 2011. http://dx.doi.org/10.1201/b14534-16.

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Conference papers on the topic "Visual opsin"

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Bybee, Seth M. "Opsin and color evolution among the most molecularly complex terrestrial visual system (Odonata)." In 2016 International Congress of Entomology. Entomological Society of America, 2016. http://dx.doi.org/10.1603/ice.2016.93359.

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Mohanty, Samarendra K., Subrata Batabyal, Sivakumar Gajjeraman, Takeharu Nagai, and Weldon Wright. "Optical stimulation and monitoring of the visual system using bioluminescent opsin (Conference Presentation)." In Optogenetics and Optical Manipulation 2018, edited by Samarendra K. Mohanty, Nitish V. Thakor, and E. Duco Jansen. SPIE, 2018. http://dx.doi.org/10.1117/12.2291754.

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Sikka, G., X. Yun, V. Tejwani, F. R. D'Alessio, M. Damarla, J. Huetsch, D. Berkowitz, and L. A. Shimoda. "Non-Visual Opsins Mediate Light-Dependent Apoptosis of Pulmonary Arterial Smooth Muscle Cells (PASMCs) in a Rat Model of Pulmonary Arterial Hypertension (PAH)." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a5061.

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