Торлы жарық сезгіш қабылдағыш ақуызы (Torly zharyq sezgish qabyldagysh aqwyzy)

Light sensitive receptor protein

the visual rhodopsin of the vertebrate [[rod cell

Rhodopsin, also known as visual purple, is a protein encoded by the RHO gene and a G protein coupled receptor (GPCR). It is the opsin of the rod cells in the retina and a light sensitive receptor protein that triggers visual phototransduction in rods. Rhodopsin mediates dim light vision and thus is extremely sensitive to light. 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. Defects in the rhodopsin gene cause eye diseases such as retinitis pigmentosa and congenital stationary night blindness.

Rhodopsin was discovered by Franz Christian Boll in 1876. The name rhodospsin derives from Ancient Greek ῥόδον for "rose", due to its pinkish color, and ὄψις for "sight". It was coined in 1878 by the German physiologist Wilhelm Friedrich Kühne (1837–1900). 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. 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. efn|Hofmann and Lamb

Rhodopsin is a protein found in the outer segment discs of rod cells. It mediates scotopic vision, which is monochromatic vision in dim light. Rhodopsin most strongly absorbs green blue light (~500 nm) 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, as well as cryptochrome (light sensitive, but not an opsin).

Rhodopsin, like other opsins, is a G protein coupled receptor (GPCR). 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. The ligand for rhodopsin is the vitamin A based chromophore 11 cis retinal, which lies horizontally to the cell membrane and is covalently bound to a lysine residue (lys296) in the seventh transmembrane domain 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, the receptor activating form, causing conformal changes in rhodopsin (bleaching), Thus, a chemoreceptor is converted to a light or photo(n)receptor. The retinal binding lysine is conserved in almost all opsins, only a few opsins having lost it during evolution. including rhodopsin. Rhodopsin is made constitutively (continuously) active by some of those mutations even without light. Also wild type rhodopsin is constitutively active, if no 11 cis retinal is bound, but much less. Therefore 11 cis retinal is an inverse agonist. Such mutations are one cause of autosomal dominant retinitis pigmentosa. The rhodopsin of cattle has 348 amino acids, the retinal binding lysine being Lys296. It was the first opsin whose amino acid sequence and 3D structure were determined. 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. 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. 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.

Rhodopsin is an essential G protein coupled receptor in phototransduction.

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 ). 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. 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.

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. 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. 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. Several other pathological states relating to rhodopsin have been discovered including poor post Golgi trafficking, dysregulative activation, rod outer segment instability and arrestin binding.