Rhodopsin

Last updated

RHO
Rhodopsin.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases RHO , CSNBAD1, OPN2, RP4, rhodopsin, Rhodopsin, visual purple
External IDs OMIM: 180380; MGI: 97914; HomoloGene: 68068; GeneCards: RHO; OMA:RHO - orthologs
Orthologs
SpeciesHumanMouse
Entrez

6010

212541

Ensembl

ENSG00000163914

ENSMUSG00000030324

UniProt

P08100

P15409

RefSeq (mRNA)

NM_000539

NM_145383

RefSeq (protein)

NP_000530

NP_663358

Location (UCSC) Chr 3: 129.53 – 129.54 Mb Chr 6: 115.91 – 115.92 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Rhodopsin, also known as visual purple, is a protein encoded by the RHO gene [5] and a G-protein-coupled receptor (GPCR). It is a light-sensitive receptor protein that triggers visual phototransduction in rods. Rhodopsin mediates dim light vision and thus is extremely sensitive to light. [6] When rhodopsin is exposed to light, it immediately photobleaches. In humans, it is regenerated fully in about 30 minutes, after which the rods are more sensitive. [7] Defects in the rhodopsin gene cause eye diseases such as retinitis pigmentosa and congenital stationary night blindness.

Contents

Names

Rhodopsin was discovered by Franz Christian Boll in 1876. [8] [9] [10] The name rhodopsin derives from Ancient Greek ῥόδον (rhódon) for "rose", due to its pinkish color, and ὄψις (ópsis) for "sight". [11] It was coined in 1878 by the German physiologist Wilhelm Friedrich Kühne (1837–1900). [12] [13]

When George Wald discovered that rhodopsin is a holoprotein, consisting of retinal and an apoprotein, he called it opsin, which today would be described more narrowly as apo-rhodopsin. [14] Today, the term opsin refers more broadly to the class of G-protein-coupled receptors that bind retinal and as a result become a light sensitive photoreceptor, including all closely related proteins. [15] [16] [17] [a] When Wald and colleagues later isolated iodopsin from chicken retinas, thereby discovering the first known cone opsin, they called apo-iodopsin photopsin (for its relation to photopic vision) and apo-rhodopsin scotopsin (for its use in scotopic vision). [18]

General

Rhodopsin is a protein found in the outer segment discs of rod cells. It mediates scotopic vision, which is monochromatic vision in dim light. [7] [19] Rhodopsin most strongly absorbs green-blue light (~500 nm) [20] [21] and appears therefore reddish-purple, hence the archaic term "visual purple".

Several closely related opsins differ only in a few amino acids and in the wavelengths of light that they absorb most strongly. Humans have, including rhodopsin, nine opsins, [15] as well as cryptochrome (light-sensitive, but not an opsin). [22]

Structure

Cattle rhodopsin Bovine rhodopsin.png
Cattle rhodopsin

Rhodopsin, like other opsins, is a G-protein-coupled receptor (GPCR). [23] [24] GPCRs are chemoreceptors that embed in the lipid bilayer of the cell membranes and have seven transmembrane domains forming a binding pocket for a ligand. [25] [26] The ligand for rhodopsin is the vitamin A-based chromophore 11-cis-retinal, [27] [28] [29] [30] [31] which lies horizontally to the cell membrane [32] and is covalently bound to a lysine residue (lys296) [33] in the seventh transmembrane domain [34] [32] through a Schiff-base. [35] [36] However, 11-cis-retinal only blocks the binding pocket and does not activate rhodopsin. It is only activated when 11-cis-retinal absorbs a photon of light and isomerizes to all-trans-retinal, [37] [38] the receptor activating form, [39] [40] causing conformal changes in rhodopsin (bleaching), [39] which activate a phototransduction cascade. [41] Thus, a chemoreceptor is converted to a light or photo(n)receptor. [16]

The retinal binding lysine is conserved in almost all opsins, only a few opsins having lost it during evolution. [16] Opsins without the lysine are not light sensitive, [42] [43] [44] including rhodopsin. Rhodopsin is made constitutively (continuously) active by some of those mutations even without light. [45] [46] [47] Also wild-type rhodopsin is constitutively active, if no 11-cis-retinal is bound, but much less. [48] Therefore 11-cis-retinal is an inverse agonist. Such mutations are one cause of autosomal dominant retinitis pigmentosa. [47] Artificially, the retinal binding lysine can be shifted to other positions, even into other transmembrane domains, without changing the activity. [49]

The rhodopsin of cattle has 348 amino acids, the retinal binding lysine being Lys296. It was the first opsin whose amino acid sequence [50] and 3D-structure were determined. [32] Its structure has been studied in detail by x-ray crystallography on rhodopsin crystals. [51] Several models (e.g., the bicycle-pedal mechanism, hula-twist mechanism) attempt to explain how the retinal group can change its conformation without clashing with the enveloping rhodopsin protein pocket. [52] [53] [54] Recent data support that rhodopsin is a functional monomer, instead of a dimer, which was the paradigm of G-protein-coupled receptors for many years. [55]

Within its native membrane, rhodopsin is found at a high density facilitating its ability to capture photons. Due to its dense packing within the membrane, there is a higher chance of rhodopsin capturing proteins. However, the high density also provides a disadvantage when it comes to G protein signaling because the diffusion becomes more difficult in a crowded membrane that is packed with the receptor, rhodopsin. [56]

Phototransduction

The visual cycle follows the renewal of the retinal chromophore. It runs in parallel to the phototransduction pathway. Visual cycle.svg
The visual cycle follows the renewal of the retinal chromophore. It runs in parallel to the phototransduction pathway.

Rhodopsin is an essential G-protein coupled receptor in phototransduction.

Activation

In rhodopsin, the aldehyde group of retinal is covalently linked to the amino group of a lysine residue on the protein in a protonated Schiff base (-NH+=CH-). [33] When rhodopsin absorbs light, its retinal cofactor isomerizes from the 11-cis to the all-trans configuration, and the protein subsequently undergoes a series of relaxations to accommodate the altered shape of the isomerized cofactor. The intermediates formed during this process were first investigated in the laboratory of George Wald, who received the Nobel prize for this research in 1967. [57] The photoisomerization dynamics has been subsequently investigated with time-resolved IR spectroscopy and UV/Vis spectroscopy. A first photoproduct called photorhodopsin forms within 200 femtoseconds after irradiation, followed within picoseconds by a second one called bathorhodopsin with distorted all-trans bonds. This intermediate can be trapped and studied at cryogenic temperatures, and was initially referred to as prelumirhodopsin. [58] In subsequent intermediates lumirhodopsin and metarhodopsin I, the Schiff's base linkage to all-trans retinal remains protonated, and the protein retains its reddish color. The critical change that initiates the neuronal excitation involves the conversion of metarhodopsin I to metarhodopsin II, which is associated with deprotonation of the Schiff's base and change in color from red to yellow. [59]

Phototransduction cascade

The product of light activation, Metarhodopsin II, initiates the visual phototransduction second messenger pathway by stimulating the G-protein transducin (Gt), resulting in the liberation of its α subunit. This GTP-bound subunit in turn activates a cGMP phosphodiesterase. The cGMP phosphodiesterase hydrolyzes (breaks down) cGMP, lowering its local concentration so it can no longer activate cGMP-dependent cation channels. This leads to the hyperpolarization of photoreceptor cells, changing the rate at which they release transmitters. [60] [41]

Deactivation

Meta II (metarhodopsin II) is deactivated rapidly after activating transducin by rhodopsin kinase and arrestin. [61] Rhodopsin pigment must be regenerated for further phototransduction to occur. This means replacing all-trans-retinal with 11-cis-retinal and the decay of Meta II is crucial in this process. During the decay of Meta II, the Schiff base link that normally holds all-trans-retinal and the apoprotein opsin (aporhodopsin) is hydrolyzed and becomes Meta III. In the rod outer segment, Meta III decays into separate all-trans-retinal and opsin. [61] A second product of Meta II decay is an all-trans-retinal opsin complex in which the all-trans-retinal has been translocated to second binding sites. Whether the Meta II decay runs into Meta III or the all-trans-retinal opsin complex seems to depend on the pH of the reaction. Higher pH tends to drive the decay reaction towards Meta III. [61]

Diseases of the retina

Mutations in the rhodopsin gene contribute majorly to various diseases of the retina such as retinitis pigmentosa. In general, the defect rhodopsin aggregates with ubiquitin in inclusion bodies, disrupts the intermediate filament network, and impairs the ability of the cell to degrade non-functioning proteins, which leads to photoreceptor apoptosis. [62] Other mutations on rhodopsin lead to X-linked congenital stationary night blindness, mainly due to constitutive activation, when the mutations occur around the chromophore binding pocket of rhodopsin. [63] Several other pathological states relating to rhodopsin have been discovered including poor post-Golgi trafficking, dysregulative activation, rod outer segment instability and arrestin binding. [63]

See also

Explanatory notes

  1. ↑ Hofmann and Lamb [17] use the term opsin in general to mean the group of opsins, however they call apo-rhodopsin in their figure 4 opsin, too.

Related Research Articles

<span class="mw-page-title-main">Retinitis pigmentosa</span> Gradual retinal degeneration leading to progressive sight loss

Retinitis pigmentosa (RP) is a member of a group of genetic disorders called inherited retinal dystrophy (IRD) that cause loss of vision. Symptoms include trouble seeing at night and decreasing peripheral vision. As peripheral vision worsens, people may experience "tunnel vision". Complete blindness is uncommon. Onset of symptoms is generally gradual and often begins in childhood.

<span class="mw-page-title-main">Retinal</span> Vitamin A aldehyde, a polyene chromophore

Retinal is a polyene chromophore. Retinal, bound to proteins called opsins, is the chemical basis of visual phototransduction, the light-detection stage of visual perception (vision).

<span class="mw-page-title-main">Melanopsin</span> Mammalian protein found in Homo sapiens

Melanopsin is a type of photopigment belonging to a larger family of light-sensitive retinal proteins called opsins and encoded by the gene Opn4. In the mammalian retina, there are two additional categories of opsins, both involved in the formation of visual images: rhodopsin and photopsin in the rod and cone photoreceptor cells, respectively.

<span class="mw-page-title-main">Opsin</span> Class of light-sensitive proteins

Animal opsins are G-protein-coupled receptors and a group of proteins made light-sensitive via a chromophore, typically retinal. When bound to retinal, opsins become retinylidene proteins, but are usually still called opsins regardless. Most prominently, they are found in photoreceptor cells of the retina. Five classical groups of opsins are involved in vision, mediating the conversion of a photon of light into an electrochemical signal, the first step in the visual transduction cascade. Another opsin found in the mammalian retina, melanopsin, is involved in circadian rhythms and pupillary reflex but not in vision. Humans have in total nine opsins. Beside vision and light perception, opsins may also sense temperature, sound, or chemicals.

Rhodopsin kinase is a serine/threonine-specific protein kinase involved in phototransduction. This enzyme catalyses the following chemical reaction:

Retinylidene proteins, or rhodopsins in a broad sense, are proteins that use retinal as a chromophore for light reception. They are the molecular basis for a variety of light-sensing systems from phototaxis in flagellates to eyesight in animals. Retinylidene proteins include all forms of opsin and rhodopsin. While rhodopsin in the narrow sense refers to a dim-light visual pigment found in vertebrates, usually on rod cells, rhodopsin in the broad sense refers to any molecule consisting of an opsin and a retinal chromophore in the ground state. When activated by light, the chromophore is isomerized, at which point the molecule as a whole is no longer rhodopsin, but a related molecule such as metarhodopsin. However, it remains a retinylidene protein. The chromophore then separates from the opsin, at which point the bare opsin is a retinylidene protein. Thus, the molecule remains a retinylidene protein throughout the phototransduction cycle.

<span class="mw-page-title-main">Photoreceptor cell-specific nuclear receptor</span> Protein-coding gene in the species Homo sapiens

The photoreceptor cell-specific nuclear receptor (PNR), also known as NR2E3, is a protein that in humans is encoded by the NR2E3 gene. PNR is a member of the nuclear receptor super family of intracellular transcription factors.

<span class="mw-page-title-main">RRH</span> Protein-coding gene in the species Homo sapiens

Peropsin, a visual pigment-like receptor, is a protein that in humans is encoded by the RRH gene. It belongs like other animal opsins to the G protein-coupled receptors. Even so, the first peropsins were already discovered in mice and humans in 1997, not much is known about them.

<span class="mw-page-title-main">Retinal G protein coupled receptor</span> Protein-coding gene in the species Homo sapiens

RPE-retinal G protein-coupled receptor also known as RGR-opsin is a protein that in humans is encoded by the RGR gene. RGR-opsin is a member of the rhodopsin-like receptor subfamily of GPCR. Like other opsins which bind retinaldehyde, it contains a conserved lysine residue in the seventh transmembrane domain. RGR-opsin comes in different isoforms produced by alternative splicing.

<span class="mw-page-title-main">Retinitis pigmentosa GTPase regulator</span> Protein found in humans

X-linked retinitis pigmentosa GTPase regulator is a GTPase-binding protein that in humans is encoded by the RPGR gene. The gene is located on the X-chromosome and is commonly associated with X-linked retinitis pigmentosa (XLRP). In photoreceptor cells, RPGR is localized in the connecting cilium which connects the protein-synthesizing inner segment to the photosensitive outer segment and is involved in the modulation of cargo trafficked between the two segments.

<span class="mw-page-title-main">Peripherin 2</span> Protein-coding gene in the species Homo sapiens

Peripherin-2 is a protein, that in humans is encoded by the PRPH2 gene. Peripherin-2 is found in the rod and cone cells of the retina of the eye. Defects in this protein result in one form of retinitis pigmentosa, an incurable blindness.

<span class="mw-page-title-main">Retinaldehyde-binding protein 1</span> Protein-coding gene in the species Homo sapiens

Retinaldehyde-binding protein 1 (RLBP1) also known as cellular retinaldehyde-binding protein (CRALBP) is a 36-kD water-soluble protein that in humans is encoded by the RLBP1 gene.

<span class="mw-page-title-main">PDE6B</span> Protein-coding gene in the species Homo sapiens

Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta is the beta subunit of the protein complex PDE6 that is encoded by the PDE6B gene. PDE6 is crucial in transmission and amplification of visual signal. The existence of this beta subunit is essential for normal PDE6 functioning. Mutations in this subunit are responsible for retinal degeneration such as retinitis pigmentosa or congenital stationary night blindness.

<span class="mw-page-title-main">SAG (gene)</span>

S-arrestin is a protein that in humans is encoded by the SAG gene.

<span class="mw-page-title-main">ARR3</span> Protein-coding gene in humans

Arrestin-C, also known as retinal cone arrestin-3, is a protein that in humans is encoded by the ARR3 gene.

<span class="mw-page-title-main">TULP1</span> Protein-coding gene in the species Homo sapiens

Tubby-related protein 1 is a protein that in humans is encoded by the TULP1 gene.

<span class="mw-page-title-main">RP1</span> Protein-coding gene in humans

Oxygen-regulated protein 1 also known as retinitis pigmentosa 1 protein (RP1) is a protein that in humans is encoded by the RP1 gene.

Retinal gene therapy holds a promise in treating different forms of non-inherited and inherited blindness.

Nematode chemoreceptors are chemoreceptors of nematodes. Animals recognise a wide variety of chemicals using their senses of taste and smell. The nematode Caenorhabditis elegans has only 14 types of chemosensory neuron, yet is able to respond to dozens of chemicals because each neuron detects several stimuli. More than 40 highly divergent transmembrane proteins that could contribute to this functional diversity have been described. Most of the candidate receptor genes are in clusters of similar genes; 11 of these appear to be expressed in small subsets of chemosensory neurons. A single type of neuron can potentially express at least 4 different receptor genes. Some of these might encode receptors for water-soluble attractants, repellents and pheromones, which are divergent members of the G-protein-coupled receptor family. Sequences of the Sra family of C. elegans receptor-like proteins contain 6-7 hydrophobic, putative transmembrane, regions. These can be distinguished from other 7TM proteins by their own characteristic TM signatures.

<span class="mw-page-title-main">Vertebrate visual opsin</span>

Vertebrate visual opsins are a subclass of ciliary opsins and mediate vision in vertebrates. They include the opsins in human rod and cone cells. They are often abbreviated to opsin, as they were the first opsins discovered and are still the most widely studied opsins.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000163914 – Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000030324 – Ensembl, May 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ↑ "RHO rhodopsin [Homo sapiens (human)]". NCBI. Retrieved 16 November 2017.
  6. ↑ Litmann BJ, Mitchell DC (1996). "Rhodopsin structure and function". In Lee AG (ed.). Rhodopsin and G-Protein Linked Receptors, Part A (Vol 2, 1996) (2 Vol Set). Biomembranes: A Multi-Volume Treatise. Vol. 2. Greenwich, Conn: JAI Press. pp. 1–32. doi:10.1016/S1874-5342(07)80004-3. ISBN   978-1-55938-659-3.
  7. 1 2 Stuart JA, Brige RR (1996). "Characterization of the primary photochemical events in bacteriorhodopsin and rhodopsin". In Lee AG (ed.). Rhodopsin and G-Protein Linked Receptors, Part A (Vol 2, 1996) (2 Vol Set). Biomembranes: A Multi-Volume Treatise. Vol. 2. Greenwich, Conn: JAI Press. pp. 33–140. doi:10.1016/S1874-5342(07)80005-5. ISBN   978-1-55938-659-3.
  8. ↑ Encyclopedia of the Neurological Sciences. Academic Press. 29 April 2014. pp. 441–. ISBN   978-0-12-385158-1.
  9. ↑ Giese AC (24 September 2013). Photophysiology: General Principles; Action of Light on Plants. Elsevier. p. 9. ISBN   978-1-4832-6227-7 . Retrieved 23 September 2015.
  10. ↑ Boll F (1877). "Zur Anatomie und Physiologie der Retina" [On the anatomy and physiology of the retina]. Archiv für Anatomie und Physiologie, Physiologische Abtheilung (in German): 4–35.
  11. ↑ "Rhodopsin: History and Etymology for rhodopsin". Merriam-Webster on-line dictionary.
  12. ↑ See:
    • Merriam-Webster Online Dictionary: Rhodopsin: History and Etymology for rhodopsin
    • Ewald A, Kühne W (1878). "Untersuchungen über den Sehpurpur" [Investigations into rhodopsin]. Untersuchungen aus dem Physiologischen Institute der Universität Heidelberg (in German). 1: 139–218. From p. 181: "Was den Sehpurpur im Dunkel ändert, pflegt es z. Th. [= zum Theil] in derselben Weise zu thun, wie das Licht, d.h. erst eine gelbe Materie, dann farblose Substanz hervorzubringen. Der Kürze wegen und um dem Auslande unsere Bezeichnungen zugänglich zu machen, kann man sagen, Rhodopsin werde erst in Xanthopsin, dieses in Leukopsin zersetzt." (That which alters visual purple in the dark usually acts to some extent in the same way as light, that is, first producing a yellow material, then a colorless substance. For the sake of brevity, and in order to make our designations more accessible to foreigners, we can say that rhodopsin is first degraded into xanthopsin [- visual yellow], and [then] this is degraded into leucopsin [- visual white].)
  13. ↑ Wade NJ (November 2008). "Visual purple (sehpurpur)". Perception. 37 (11): 1617–1620. doi:10.1068/p3711ed. PMID   19189727. S2CID   19145558.
  14. ↑ Wald G (December 1951). "The photochemical basis of rod vision". Journal of the Optical Society of America. 41 (12): 949–956. Bibcode:1951JOSA...41..949W. doi:10.1364/josa.41.000949. PMID   14908734.
  15. 1 2 Terakita A (2005). "The opsins". Genome Biology. 6 (3): 213. doi: 10.1186/gb-2005-6-3-213 . PMC   1088937 . PMID   15774036.
  16. 1 2 3 Gühmann M, Porter ML, Bok MJ (August 2022). "The Gluopsins: Opsins without the Retinal Binding Lysine". Cells. 11 (15): 2441. doi: 10.3390/cells11152441 . PMC   9368030 . PMID   35954284. CC-BY icon.svg Material was copied and adapted from this source, which is available under a Creative Commons Attribution 4.0 International License.
  17. 1 2 Hofmann KP, Lamb TD (March 2023). "Rhodopsin, light-sensor of vision". Progress in Retinal and Eye Research. 93: 101116. doi: 10.1016/j.preteyeres.2022.101116 . PMID   36273969. S2CID   253041556.
  18. ↑ Wald G, Brown PK, Smith PH (May 1955). "Iodopsin". The Journal of General Physiology. 38 (5): 623–681. doi:10.1085/jgp.38.5.623. PMC   2147498 . PMID   14367777.
  19. ↑ Rogers K. "Rhodopsin". Encyclopædia Britannica. Britannica.com. Retrieved 30 January 2016.
  20. ↑ Wald G, Brown PK (January 1958). "Human rhodopsin". Science. 127 (3292): 222–226. Bibcode:1958Sci...127..222W. doi:10.1126/science.127.3292.222. PMID   13495499. S2CID   45459123.
  21. ↑ Bowmaker JK, Dartnall HJ (January 1980). "Visual pigments of rods and cones in a human retina". The Journal of Physiology. 298 (1): 501–511. doi:10.1113/jphysiol.1980.sp013097. PMC   1279132 . PMID   7359434.
  22. ↑ Foley LE, Gegear RJ, Reppert SM (June 2011). "Human cryptochrome exhibits light-dependent magnetosensitivity". Nature Communications. 2: 356. Bibcode:2011NatCo...2..356F. doi:10.1038/ncomms1364. PMC   3128388 . PMID   21694704.
  23. ↑ Casey PJ, Gilman AG (February 1988). "G protein involvement in receptor-effector coupling". The Journal of Biological Chemistry. 263 (6): 2577–2580. doi: 10.1016/s0021-9258(18)69103-3 . PMID   2830256. S2CID   38970721.
  24. ↑ Attwood TK, Findlay JB (February 1994). "Fingerprinting G-protein-coupled receptors". Protein Engineering. 7 (2): 195–203. doi:10.1093/protein/7.2.195. PMID   8170923.
  25. ↑ Dixon RA, Kobilka BK, Strader DJ, Benovic JL, Dohlman HG, Frielle T, et al. (May 1986). "Cloning of the gene and cDNA for mammalian beta-adrenergic receptor and homology with rhodopsin". Nature. 321 (6065): 75–79. Bibcode:1986Natur.321...75D. doi:10.1038/321075a0. PMID   3010132. S2CID   4324074.
  26. ↑ Dixon RA, Sigal IS, Rands E, Register RB, Candelore MR, Blake AD, et al. (March 1987). "Ligand binding to the beta-adrenergic receptor involves its rhodopsin-like core". Nature. 326 (6108): 73–77. Bibcode:1987Natur.326...73D. doi:10.1038/326073a0. PMID   2881211. S2CID   4352920.
  27. ↑ Wald G (July 1934). "Carotenoids and the Vitamin A Cycle in Vision". Nature. 134 (3376): 65. Bibcode:1934Natur.134...65W. doi: 10.1038/134065a0 . S2CID   4022911.
  28. ↑ Wald G, Brown PK, Hubbard R, Oroshnik W (July 1955). "Hindered Cis Isomers of Vitamin a and Retinene: The Structure of the Neo-B Isomer". Proceedings of the National Academy of Sciences of the United States of America. 41 (7): 438–451. Bibcode:1955PNAS...41..438W. doi: 10.1073/pnas.41.7.438 . PMC   528115 . PMID   16589696.
  29. ↑ Brown PK, Wald G (October 1956). "The neo-b isomer of vitamin A and retinene". The Journal of Biological Chemistry. 222 (2): 865–877. doi: 10.1016/S0021-9258(20)89944-X . PMID   13367054.
  30. ↑ Oroshnik W (June 1956). "The Synthesis and Configuration of Neo-B Vitamin A and Neoretinine b". Journal of the American Chemical Society. 78 (11): 2651–2652. doi:10.1021/ja01592a095.
  31. ↑ Oroshnik W, Brown PK, Hubbard R, Wald G (September 1956). "HINDERED CIS ISOMERS OF VITAMIN A AND RETINENE: THE STRUCTURE OF THE NEO-b ISOMER". Proceedings of the National Academy of Sciences of the United States of America. 42 (9): 578–580. Bibcode:1956PNAS...42..578O. doi: 10.1073/pnas.42.9.578 . PMC   534254 . PMID   16589909.
  32. 1 2 3 Palczewski K, Kumasaka T, Hori T, Behnke CA, Motoshima H, Fox BA, et al. (August 2000). "Crystal structure of rhodopsin: A G protein-coupled receptor". Science. 289 (5480): 739–745. Bibcode:2000Sci...289..739P. CiteSeerX   10.1.1.1012.2275 . doi:10.1126/science.289.5480.739. PMID   10926528.
  33. 1 2 Bownds D (December 1967). "Site of attachment of retinal in rhodopsin". Nature. 216 (5121): 1178–1181. Bibcode:1967Natur.216.1178B. doi:10.1038/2161178a0. PMID   4294735. S2CID   1657759.
  34. ↑ Hargrave PA, McDowell JH, Curtis DR, Wang JK, Juszczak E, Fong SL, et al. (1983). "The structure of bovine rhodopsin". Biophysics of Structure and Mechanism. 9 (4): 235–244. doi:10.1007/BF00535659. PMID   6342691. S2CID   20407577.
  35. ↑ Collins FD (March 1953). "Rhodopsin and indicator yellow". Nature. 171 (4350): 469–471. Bibcode:1953Natur.171..469C. doi:10.1038/171469a0. PMID   13046517. S2CID   4152360.
  36. ↑ Pitt GA, Collins FD, Morton RA, Stok P (January 1955). "Studies on rhodopsin. VIII. Retinylidenemethylamine, an indicator yellow analogue". The Biochemical Journal. 59 (1): 122–128. doi:10.1042/bj0590122. PMC   1216098 . PMID   14351151.
  37. ↑ Hubbard R, Kropf A (February 1958). "The Action of Light on Rhodopsin". Proceedings of the National Academy of Sciences of the United States of America. 44 (2): 130–139. Bibcode:1958PNAS...44..130H. doi: 10.1073/pnas.44.2.130 . PMC   335377 . PMID   16590155.
  38. ↑ Kropf A, Hubbard R (November 1959). "The mechanism of bleaching rhodopsin". Annals of the New York Academy of Sciences. 74 (2): 266–280. Bibcode:1959NYASA..74..266K. doi:10.1111/j.1749-6632.1958.tb39550.x. PMID   13627857. S2CID   45830716.
  39. 1 2 Choe HW, Kim YJ, Park JH, Morizumi T, Pai EF, Krauss N, et al. (March 2011). "Crystal structure of metarhodopsin II". Nature. 471 (7340): 651–655. Bibcode:2011Natur.471..651C. doi:10.1038/nature09789. PMID   21389988. S2CID   4302421.
  40. ↑ Wald G (October 1968). "Molecular basis of visual excitation". Science. 162 (3850): 230–239. Bibcode:1968Sci...162..230W. doi:10.1126/science.162.3850.230. PMID   4877437.
  41. 1 2 Terakita A, Kawano-Yamashita E, Koyanagi M (January 2012). "Evolution and diversity of opsins". Wiley Interdisciplinary Reviews: Membrane Transport and Signaling. 1 (1): 104–111. doi: 10.1002/wmts.6 .
  42. ↑ Katana R, Guan C, Zanini D, Larsen ME, Giraldo D, Geurten BR, et al. (September 2019). "Chromophore-Independent Roles of Opsin Apoproteins in Drosophila Mechanoreceptors". Current Biology. 29 (17): 2961–2969.e4. Bibcode:2019CBio...29E2961K. doi: 10.1016/j.cub.2019.07.036 . PMID   31447373. S2CID   201420079.
  43. ↑ Leung NY, Thakur DP, Gurav AS, Kim SH, Di Pizio A, Niv MY, et al. (April 2020). "Functions of Opsins in Drosophila Taste". Current Biology. 30 (8): 1367–1379.e6. Bibcode:2020CBio...30E1367L. doi:10.1016/j.cub.2020.01.068. PMC   7252503 . PMID   32243853.
  44. ↑ Kumbalasiri T, Rollag MD, Isoldi MC, Castrucci AM, Provencio I (March 2007). "Melanopsin triggers the release of internal calcium stores in response to light". Photochemistry and Photobiology. 83 (2): 273–279. doi:10.1562/2006-07-11-RA-964. PMID   16961436. S2CID   23060331.
  45. ↑ Robinson PR, Cohen GB, Zhukovsky EA, Oprian DD (October 1992). "Constitutively active mutants of rhodopsin". Neuron. 9 (4): 719–725. doi:10.1016/0896-6273(92)90034-b. PMID   1356370. S2CID   13172583.
  46. ↑ Yang T, Snider BB, Oprian DD (December 1997). "Synthesis and characterization of a novel retinylamine analog inhibitor of constitutively active rhodopsin mutants found in patients with autosomal dominant retinitis pigmentosa". Proceedings of the National Academy of Sciences of the United States of America. 94 (25): 13559–13564. Bibcode:1997PNAS...9413559Y. doi: 10.1073/pnas.94.25.13559 . PMC   28345 . PMID   9391065.
  47. 1 2 Park PS (2014). "Constitutively active rhodopsin and retinal disease". Pharmacology & Therapeutics of Constitutively Active Receptors. Advances in Pharmacology. Vol. 70. pp. 1–36. doi:10.1016/B978-0-12-417197-8.00001-8. ISBN   978-0-12-417197-8. PMC   4120657 . PMID   24931191.
  48. ↑ Melia TJ, Cowan CW, Angleson JK, Wensel TG (December 1997). "A comparison of the efficiency of G protein activation by ligand-free and light-activated forms of rhodopsin". Biophysical Journal. 73 (6): 3182–3191. Bibcode:1997BpJ....73.3182M. doi:10.1016/S0006-3495(97)78344-9. PMC   1181221 . PMID   9414230.
  49. ↑ Devine EL, Oprian DD, Theobald DL (August 2013). "Relocating the active-site lysine in rhodopsin and implications for evolution of retinylidene proteins". Proceedings of the National Academy of Sciences of the United States of America. 110 (33): 13351–13355. Bibcode:2013PNAS..11013351D. doi: 10.1073/pnas.1306826110 . PMC   3746867 . PMID   23904486.
  50. ↑ Ovchinnikov YA (November 1982). "Rhodopsin and bacteriorhodopsin: structure-function relationships". FEBS Letters. 148 (2): 179–191. doi: 10.1016/0014-5793(82)80805-3 . PMID   6759163. S2CID   85819100.
  51. ↑ Gulati S, Jastrzebska B, Banerjee S, Placeres ÁL, Miszta P, Gao S, et al. (March 2017). "Photocyclic behavior of rhodopsin induced by an atypical isomerization mechanism". Proceedings of the National Academy of Sciences of the United States of America. 114 (13): E2608–E2615. Bibcode:2017PNAS..114E2608G. doi: 10.1073/pnas.1617446114 . PMC   5380078 . PMID   28289214.
  52. ↑ Nakamichi H, Okada T (June 2006). "Crystallographic analysis of primary visual photochemistry". Angewandte Chemie. 45 (26): 4270–4273. doi:10.1002/anie.200600595. PMID   16586416.
  53. ↑ Schreiber M, Sugihara M, Okada T, Buss V (June 2006). "Quantum mechanical studies on the crystallographic model of bathorhodopsin". Angewandte Chemie. 45 (26): 4274–4277. doi:10.1002/anie.200600585. PMID   16729349.
  54. ↑ Weingart O (September 2007). "The twisted C11=C12 bond of the rhodopsin chromophore--a photochemical hot spot". Journal of the American Chemical Society. 129 (35): 10618–10619. doi:10.1021/ja071793t. PMID   17691730.
  55. ↑ Chabre M, le Maire M (July 2005). "Monomeric G-protein-coupled receptor as a functional unit". Biochemistry. 44 (27): 9395–9403. doi:10.1021/bi050720o. PMID   15996094.
  56. ↑ Park PS (October 2019). "Rhodopsin Oligomerization and Aggregation". The Journal of Membrane Biology. 252 (4–5): 413–423. doi:10.1007/s00232-019-00078-1. PMC   6790290 . PMID   31286171.
  57. ↑ The Nobel Foundation. "The Nobel Prize in Physiology or Medicine 1967". Nobelprize.org. Nobel Media AB 2014. Retrieved 12 December 2015.
  58. ↑ Yoshizawa T, Wald G (March 1963). "Pre-lumirhodopsin and the bleaching of visual pigments". Nature. 197 (Mar 30): 1279–1286. Bibcode:1963Natur.197.1279Y. doi:10.1038/1971279a0. PMID   14002749. S2CID   4263392.
  59. ↑ Matthews RG, Hubbard R, Brown PK, Wald G (November 1963). "Tautomeric Forms of Metarhodopsin". The Journal of General Physiology. 47 (2): 215–240. doi:10.1085/jgp.47.2.215. PMC   2195338 . PMID   14080814.
  60. ↑ Hofmann KP, Heck M (1996). "Light-induced protein-protein interactions on the rod photoreceptor disc membrane". In Lee AG (ed.). Rhodopsin and G-Protein Linked Receptors, Part A (Vol 2, 1996) (2 Vol Set). Biomembranes: A Multi-Volume Treatise. Vol. 2. Greenwich, Conn: JAI Press. pp. 141–198. doi:10.1016/S1874-5342(07)80006-7. ISBN   978-1-55938-659-3.
  61. 1 2 3 Heck M, Schädel SA, Maretzki D, Bartl FJ, Ritter E, Palczewski K, et al. (January 2003). "Signaling states of rhodopsin. Formation of the storage form, metarhodopsin III, from active metarhodopsin II". The Journal of Biological Chemistry. 278 (5): 3162–3169. doi: 10.1074/jbc.M209675200 . PMC   1364529 . PMID   12427735.
  62. ↑ Saliba RS, Munro PM, Luthert PJ, Cheetham ME (July 2002). "The cellular fate of mutant rhodopsin: quality control, degradation and aggresome formation". Journal of Cell Science. 115 (Pt 14): 2907–2918. doi:10.1242/jcs.115.14.2907. PMID   12082151.
  63. 1 2 Mendes HF, van der Spuy J, Chapple JP, Cheetham ME (April 2005). "Mechanisms of cell death in rhodopsin retinitis pigmentosa: implications for therapy". Trends in Molecular Medicine. 11 (4): 177–185. doi:10.1016/j.molmed.2005.02.007. PMID   15823756.

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