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Rhodopsin Kinase
Rhodopsin kinase (, ''rod opsin kinase'', ''G-protein-coupled receptor kinase 1'', ''GPCR kinase 1'', ''GRK1'', ''opsin kinase'', ''opsin kinase (phosphorylating)'', ''rhodopsin kinase (phosphorylating)'', ''RK'', ''STK14'') is a serine/threonine-specific protein kinase involved in phototransduction. This enzyme catalyses the following chemical reaction: : ATP + rhodopsin \rightleftharpoons ADP + phospho-rhodopsin Mutations in rhodopsin kinase are associated with a form of night blindness called Oguchi disease. Function and mechanism of action Rhodopsin kinase is a member of the family of G protein-coupled receptor kinases, and is officially named G protein-coupled receptor kinase 1, or GRK1. Rhodopsin kinase is found primarily in mammalian retinal rod cells, where it phosphorylates light-activated rhodopsin, a member of the family of G protein-coupled receptors that recognizes light. Phosphorylated, light-activated rhodopsin binds to the protein arrestin to terminate the lig ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Serine/threonine-specific Protein Kinase
A serine/threonine protein kinase () is a kinase enzyme, in particular a protein kinase, that phosphorylates the OH group of the amino-acid residues serine or threonine, which have similar side chains. At least 350 of the 500+ human protein kinases are serine/threonine kinases (STK). In enzymology, the term ''serine/threonine protein kinase'' describes a class of enzymes in the family of transferases, that transfer phosphates to the oxygen atom of a serine or threonine side chain in proteins. This process is called phosphorylation. Protein phosphorylation in particular plays a significant role in a wide range of cellular processes and is a very important posttranslational modification. The chemical reaction performed by these enzymes can be written as :ATP + a protein \rightleftharpoons ADP + a phosphoprotein Thus, the two substrates of this enzyme are ATP and a protein, whereas its two products are ADP and phosphoprotein. The systematic name of this enzyme class ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Farnesylation
Prenylation (also known as isoprenylation or lipidation) is the addition of hydrophobic molecules to a protein or a biomolecule. It is usually assumed that prenyl groups (3-methylbut-2-en-1-yl) facilitate attachment to cell membranes, similar to lipid anchors like the GPI anchor, though direct evidence of this has not been observed. Prenyl groups (also called isoprenyl groups, having one hydrogen atom more than isoprene) have been shown to be important for protein–protein binding through specialized prenyl-binding domains. Protein prenylation Protein prenylation involves the transfer of either a farnesyl or a geranylgeranyl moiety to C-terminal cysteine(s) of the target protein. There are three enzymes that carry out prenylation in the cell, farnesyl transferase, Caax protease and geranylgeranyl transferase I. Farnesylation is a type of prenylation, a post-translational modification of proteins by which an isoprenyl group is added to a cysteine residue. It is an important p ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
G-protein Coupled Receptor Kinases
G protein-coupled receptor kinases (GPCRKs, GRKs) are a family of protein kinases within the AGC (protein kinase A, protein kinase G, protein kinase C) group of kinases. Like all AGC kinases, GRKs use ATP to add phosphate to Serine and Threonine residues in specific locations of target proteins. In particular, GRKs phosphorylate intracellular domains of G protein-coupled receptors (GPCRs). GRKs function in tandem with arrestin proteins to regulate the sensitivity of GPCRs for stimulating downstream heterotrimeric G protein and G protein-independent signaling pathways. Types of GRKs GRK Activity and Regulation GRKs reside normally in an inactive state, but their kinase activity is stimulated by binding to a ligand-activated GPCR (rather than by regulatory phosphorylation as is common in other AGC kinases). Because there are only seven GRKs (only 4 of which are widely expressed throughout the body) but over 800 human GPCRs, GRKs appear to have limited phosphorylation sit ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Rhodopsin
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. Names Rhodopsin was discovered by Franz Christian Boll in 1876. The name rhodospsin derives from Ancient Greek () for "rose", due to its pinkish color, and () 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, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Photoreceptor Cell
A photoreceptor cell is a specialized type of neuroepithelial cell found in the retina that is capable of visual phototransduction. The great biological importance of photoreceptors is that they convert light (visible electromagnetic radiation) into signals that can stimulate biological processes. To be more specific, photoreceptor proteins in the cell absorb photons, triggering a change in the cell's membrane potential. There are currently three known types of photoreceptor cells in mammalian eyes: rods, cones, and intrinsically photosensitive retinal ganglion cells. The two classic photoreceptor cells are rods and cones, each contributing information used by the visual system to form an image of the environment, sight. Rods primarily mediate scotopic vision (dim conditions) whereas cones primarily mediate to photopic vision (bright conditions), but the processes in each that supports phototransduction is similar. A third class of mammalian photoreceptor cell was di ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Visual Phototransduction
Visual phototransduction is the sensory transduction process of the visual system by which light is detected to yield nerve impulses in the rod cells and cone cells in the retina of the eye in humans and other vertebrates. It relies on the visual cycle, a sequence of biochemical reactions in which a molecule of retinal bound to opsin undergoes photoisomerization, initiates a cascade that signals detection of the photon, and is indirectly restored to its photosensitive isomer for reuse. Phototransduction in some invertebrates such as fruit flies relies on similar processes. Photoreceptors The photoreceptor cells involved in vertebrate vision are the rods, the cones, and the photosensitive ganglion cells (ipRGCs). These cells contain a chromophore ( 11-''cis''-retinal, the aldehyde of vitamin A1 and light-absorbing portion) that is bound to a cell membrane protein, opsin. Rods deal with low light level and do not mediate color vision. Cones, on the other hand, can code the c ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Retinopathy
Retinopathy is any damage to the retina of the eyes, which may cause vision impairment. Retinopathy often refers to retinal vascular disease, or damage to the retina caused by abnormal blood flow. Age-related macular degeneration is technically included under the umbrella term retinopathy but is often discussed as a separate entity. Retinopathy, or retinal vascular disease, can be broadly categorized into proliferative and non-proliferative types. Frequently, retinopathy is an ocular manifestation of systemic disease as seen in diabetes or hypertension. Diabetes is the most common cause of retinopathy in the U.S. as of 2008. Diabetic retinopathy is the leading cause of blindness in working-aged people. It accounts for about 5% of blindness worldwide and is designated a priority eye disease by the World Health Organization. Signs and symptoms Many people often do not have symptoms until very late in their disease course. Patients often become symptomatic when there is irreversibl ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Congenital Stationary Night Blindness
Congenital stationary night blindness (CSNB) is a rare non-progressive retinal disorder. People with CSNB often have difficulty adapting to low light situations due to impaired photoreceptor transmission. These patients may also have reduced visual acuity, myopia, nystagmus, and strabismus. CSNB has two forms -- complete, also known as type-1 (CSNB1), and incomplete, also known as type-2 (CSNB2), which are distinguished by the involvement of different retinal pathways. In CSNB1, downstream neurons called bipolar cells are unable to detect neurotransmission from photoreceptor cells. CSNB1 can be caused by mutations in various genes involved in neurotransmitter detection, including ''NYX''. In CSNB2, the photoreceptors themselves have impaired neurotransmission function; this is caused primarily by mutations in the gene '' CACNA1F'', which encodes a voltage-gated calcium channel important for neurotransmitter release. CSNB has been identified in horses and dogs as the result of m ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
N-terminus
The N-terminus (also known as the amino-terminus, NH2-terminus, N-terminal end or amine-terminus) is the start of a protein or polypeptide, referring to the free amine group (-NH2) located at the end of a polypeptide. Within a peptide, the amine group is bonded to the carboxylic group of another amino acid, making it a chain. That leaves a free carboxylic group at one end of the peptide, called the C-terminus, and a free amine group on the other end called the N-terminus. By convention, peptide sequences are written N-terminus to C-terminus, left to right (in LTR writing systems). This correlates the translation direction to the text direction, because when a protein is translated from messenger RNA, it is created from the N-terminus to the C-terminus, as amino acids are added to the carboxyl end of the protein. Chemistry Each amino acid has an amine group and a carboxylic group. Amino acids link to one another by peptide bonds which form through a dehydration reaction that ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Recoverin
Recoverin (abbreviated Recov) is a 23 kilodalton (kDa) neuronal calcium-binding protein that is primarily detected in the photoreceptor cells of the eye. It plays a key role in the inhibition of rhodopsin kinase, a molecule which regulates the phosphorylation of rhodopsin. A reduction in this inhibition helps regulate sensory adaptation in the retina, since the light-dependent channel closure in photoreceptors causes calcium levels to decrease, which relieves the inhibition of rhodopsin kinase by calcium-bound recoverin, leading to a more rapid inactivation of metarhodopsin II (activated form of rhodopsin). Structure & Function Recoverin is involved in the recovery phase of visual excitation and in adaptation to background light. It controls the life span of photoexcited rhodopsin by helping to inhibit rhodopsin kinase. An image of bovine recoverin with 3.00 Å resolution is shown.; This three-dimensional structure was determined by X-ray diffraction. Covalently attached at t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Visual Phototransduction
Visual phototransduction is the sensory transduction process of the visual system by which light is detected to yield nerve impulses in the rod cells and cone cells in the retina of the eye in humans and other vertebrates. It relies on the visual cycle, a sequence of biochemical reactions in which a molecule of retinal bound to opsin undergoes photoisomerization, initiates a cascade that signals detection of the photon, and is indirectly restored to its photosensitive isomer for reuse. Phototransduction in some invertebrates such as fruit flies relies on similar processes. Photoreceptors The photoreceptor cells involved in vertebrate vision are the rods, the cones, and the photosensitive ganglion cells (ipRGCs). These cells contain a chromophore ( 11-''cis''-retinal, the aldehyde of vitamin A1 and light-absorbing portion) that is bound to a cell membrane protein, opsin. Rods deal with low light level and do not mediate color vision. Cones, on the other hand, can code the c ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Transducin
Transducin (Gt) is a protein naturally expressed in vertebrate retina rods and cones and it is very important in vertebrate phototransduction. It is a type of heterotrimeric G-protein with different α subunits in rod and cone photoreceptors. Light leads to conformational changes in rhodopsin, which in turn leads to the activation of transducin. Transducin activates phosphodiesterase, which results in the breakdown of cyclic guanosine monophosphate (cGMP). The intensity of the flash response is directly proportional to the number of transducin activated. Function in phototransduction Transducin is activated by metarhodopsin II, a conformational change in rhodopsin caused by the absorption of a photon by the rhodopsin moiety retinal. The light causes isomerization of retinal from 11-cis to all-trans. Isomerization causes a change in the opsin to become metarhodopsin II. When metarhodopsin activates transducin, the guanosine diphosphate (GDP) bound to the α subunit (Tα) is ex ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
