Cyp27c1 Red-Shifts the Spectral Sensitivity of Photoreceptors by Converting Vitamin A1 into A2

Enright, Jennifer M.; Toomey, Matthew B.; Sato, Shin; Temple, Shelby E.; Allen, James H.; Fujiwara, Rina; Kramlinger, Valerie M.; Nagy, Leslie D.; Johnson, Kevin M.; Xiao, Yi; How, Martin J.; Johnson, Stephen L.; Roberts, Nicholas W.; Kefalov, Vladimir J.; Guengerich, F. Peter; Corbo, Joseph C.

doi:10.1016/j.cub.2015.10.018

Cited by 140 publications

(147 citation statements)

References 48 publications

(72 reference statements)

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“…In some vertebrates, the visual pigment’s chromophore can also tune the spectral sensitivity. Substitution of 11-cis retinal with 11-cis 3,4 didehydroretinal in photoreceptors of the eyes of zebrafish and bullfrogs cause a red-shifted sensitivity, most likely an adaption for vision under or into water [40]. Different types of chromophores, the retinal and two enantiomers of 3-hydroxyretinal have been described in insects, the latter causing a slight shift (4-12nm) towards shorter wavelengths relative to retinal [33].…”

Section: Spectral Tuning To Enhance Color Discriminationmentioning

confidence: 99%

Retinal perception and ecological significance of color vision in insects

Lebhardt

Desplan

2017

Current Opinion in Insect Science

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Color vision relies on the ability to discriminate different wavelengths and is often improved in insects that inhabit well-lit, spectrally rich environments. Although the Opsin proteins themselves are sensitive to specific wavelength ranges, other factors can alter and further restrict the sensitivity of photoreceptors to allow for finer color discrimination and thereby more informed decisions while interacting with the environment. The ability to discriminate colors differs between insects that exhibit different life styles, between female and male eyes of the same species, and between regions of the same eye, depending on the requirements of intraspecific communication and ecological demands.

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Section: Spectral Tuning To Enhance Color Discriminationmentioning

confidence: 99%

Retinal perception and ecological significance of color vision in insects

Lebhardt

Desplan

2017

Current Opinion in Insect Science

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“…Bovine adrenodoxin was expressed in Escherichia coli DH5␣ cells with the expression plasmid pBA1159 (35,36). Bovine NADPH-adrenodoxin reductase was expressed in E. coli JM109 cells as described (36,37), using a pCWori ϩ expression vector (38).…”

Section: Methodsmentioning

confidence: 99%

Specificity of Protein Covalent Modification by the Electrophilic Proteasome Inhibitor Carfilzomib in Human Cells

Federspiel

Codreanu

Goyal

et al. 2016

Molecular & Cellular Proteomics

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Carfilzomib (CFZ) is a second-generation proteasome inhibitor that is Food and Drug Administration and European Commission approved for the treatment of relapsed or refractory multiple myeloma. CFZ is an epoxomicin derivative with an epoxyketone electrophilic warhead that irreversibly adducts the catalytic threonine residue of the ␤5 subunit of the proteasome. Although CFZ produces a highly potent, sustained inactivation of the proteasome, the electrophilic nature of the drug could potentially produce off-target protein adduction. To address this possibility, we synthesized an alkynyl analog of CFZ and investigated protein adduction by this analog in HepG2 cells. Using click chemistry coupled with streptavidin based IP and shotgun tandem mass spectrometry (MS/MS), we identified two off-target proteins, cytochrome P450 27A1 (CYP27A1) and glutathione S-transferase omega 1 (GSTO1), as targets of the alkynyl CFZ probe. We confirmed the adduction of CYP27A1 and GSTO1 by streptavidin capture and immunoblotting methodology and then site-specifically mapped the adducts with targeted MS/MS methods. Although CFZ adduction of CYP27A1 and GSTO1 in vitro decreased the activities of these enzymes, the small fraction of these proteins modified by CFZ in intact cells should limit the impact of these offtarget modifications. The data support the high selectivity of CFZ for covalent modification of its therapeutic targets, despite the presence of a reactive electrophile. The approach we describe offers a generalizable method to evaluate the safety profile of covalent protein-modifying

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“…A cornerstone of this is knowledge of the photosensitivity of visual pigments, members of the large family of G-protein-coupled-receptor (GPCR) proteins, which share a common arrangement of an opsin protein linked to a chromophore derived from vitamin A (Wald 1968). Visual pigments play a core role in photon detection and color vision and they are a leading example of how gene duplications (Dulai et al 1999) and changes in amino acid sequences (Yokoyama 2008), type of chromophore (vitamin A 1 or A 2 : Enright et al 2015) and gene expression (Hofmann and Carleton 2009;Carleton et al 2010) underlie adaptations to differing ecological and behavioral selection pressures. Visual opsins in some vertebrates have been studied intensely over the past 20 years, to the extent that changes in specific ("spectral tuning") amino acid sites are known to change the peak absorbance wavelength (k max ) of the visual pigments (Yokoyama 2008;Yokoyama et al 2014).…”

Section: Introductionmentioning

confidence: 99%

Visual Pigments, Ocular Filters and the Evolution of Snake Vision

et al. 2016

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Much of what is known about the molecular evolution of vertebrate vision comes from studies of mammals, birds and fish. Reptiles (especially snakes) have barely been sampled in previous studies despite their exceptional diversity of retinal photoreceptor complements. Here, we analyze opsin gene sequences and ocular media transmission for up to 69 species to investigate snake visual evolution. Most snakes express three visual opsin genes (rh1, sws1, and lws). These opsin genes (especially rh1 and sws1) have undergone much evolutionary change, including modifications of amino acid residues at sites of known importance for spectral tuning, with several tuning site combinations unknown elsewhere among vertebrates. These changes are particularly common among dipsadine and colubrine "higher" snakes. All three opsin genes are inferred to be under purifying selection, though dN/dS varies with respect to some lineages, ecologies, and retinal anatomy. Positive selection was inferred at multiple sites in all three opsins, these being concentrated in transmembrane domains and thus likely to have a substantial effect on spectral tuning and other aspects of opsin function. Snake lenses vary substantially in their spectral transmission. Snakes active at night and some of those active by day have very transmissive lenses, whereas some primarily diurnal species cut out shorter wavelengths (including UVA). In terms of retinal anatomy, lens transmission, visual pigment spectral tuning and opsin gene evolution the visual system of snakes is exceptionally diverse compared with all other extant tetrapod orders.

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Cyp27c1 Red-Shifts the Spectral Sensitivity of Photoreceptors by Converting Vitamin A1 into A2

Cited by 140 publications

References 48 publications

Retinal perception and ecological significance of color vision in insects

Retinal perception and ecological significance of color vision in insects

Specificity of Protein Covalent Modification by the Electrophilic Proteasome Inhibitor Carfilzomib in Human Cells

Visual Pigments, Ocular Filters and the Evolution of Snake Vision

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