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Topic: Rhodopsin

Related Topics

Bacteriorhodopsin

G protein

Photopsin

Opsin

Transmembrane receptor

Photoreceptor

Integral membrane protein

Phosphorylation

Pigment

Xanthophyll

Cyclic AMP

Chemical conformation

Adenylate cyclase

Anthocyanin

Rod cell

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	rhodopsin photography
		photographs taken by rhodopsin (unless otherwise stated) CRB Disclosure issued 2005 (copies issued upon request)
		permission should be requested for the use of all rhodopsin photographs.
		All photographs are © rhodopsin photography 2004 2005 2006 2007 unless otherwise stated
	rhodopsin.co.uk (50 words)

	rhodopsin (Site not responding. Last check: 2007-10-29)
		Rhodopsin is the light absorbing pigment that is found in the rod cells.
		Rhodopsin is also known as "visual purple" because it has a maximum absorbance of 495 nm, which is in the green region of the visible spectrum.
		The alpha helices of rhodopsin are irregular in length and orientation.
	www.sas.upenn.edu /~basehore/rhodopsin.html (642 words)

	Rhodopsin - Wikipedia, the free encyclopedia
		Rhodopsin, also known as visual purple, is expressed in vertebrate photoreceptor cells.
		The structure of rhodopsin consists of a bundle of seven transmembrane helices that surround the photoreactive chromophore, 11-cis retinal.
		Rhodopsin of the rods most strongly absorbs green-blue light and therefore appears reddish-purple, which is why it is also called "visual purple".
	en.wikipedia.org /wiki/Rhodopsin (383 words)

	Rhodopsin: Genetic Music
		Rhodopsin is the protein component of the light receptor in the retinal rods of the vertebrate eye.
		A bacterial form of rhodopsin is used as a light absorbing molecule for photosynthesis.
		Duplication and modification of the rhodopsin gene seems to be the origin of the three receptor pigments responsible for color vision.
	www.whozoo.org /mac/Music/rhodopsin.htm (320 words)

	RedOrbit - Science - Phosphatidylethanolamine Enhances Rhodopsin Photoactivation and Transducin Binding in a Solid ... (Site not responding. Last check: 2007-10-29)
		MII is the conformation of the photoisomerized rhodopsin that binds and activates transducin.
		After rhodopsin was incorporated into the lipid bilayer and the PWR spectra stabilized (i.e., an equilibrium condition was reached), the aqueous compartment of the PWR cell was illuminated with yellow light (wavelength >500 nm) from a 150-W tungsten-halogen light source using a fiberoptic light guide (Fostec, Auburn, NY).
		Moreover, when rhodopsin was exposed to light the changes in the resonance positions in the PWR spectra were significantly smaller at pH 5 (8 mdeg and 5 mdeg for p- and s-polarization, respectively) compared to the shifts observed in the case of egg PC films at the same pH (cf.
	www.redorbit.com /news/display?id=123216 (8580 words)

	retinalandrhodopsin
		Rhodopsin, found in humans and other organisms, is a 40kD cross membrane protein with 7α helices and 348 amino acids.
		Rhodopsin in human rod cells is bound to scotopsin, an opsin protein.
		Rhodopsins are easily excited by light as they are conjugated systems that absorb in the visual range (28).
	www.sas.upenn.edu /~tareilaj/retinalandrhodopsin.html (412 words)

	Rhodopsin Biosynthesis and Transport (Site not responding. Last check: 2007-10-29)
		Rhodopsin is the major protein of the rod outer segment (ROS), a cellular domain which captures light and initiates the visual response.
		Rhodopsin is made in the rod inner segment (RIS) and is transported from there to the ROS on small membrane spheres called vesicles.
		Using the XOP-GFP or XOP-GFP-CT constructs, the GFP is localized to the rod inner segment (IS), nucleus and synapse.
	www.uchc.edu /dsp/rho1.html (384 words)

	Rhodopsin and the eye
		However, Rhodopsin is destroyed by bleaching on exposure to light and therefore rod cells only work in low light as at high illumination the reduced level of this photosensitive pigment leads to a very low sensitivity.
		There are many flat discs of rhodopsin within the outer segment of a rod cell which upon light detection undergo a photo-isomeric change from Rhodopsin (11-cis) to all-trans retinal.
		Photoexcited Rhodopsin (4th of the 5 intermediates) triggers an enzymatic cascade process resulting in the hydrolysis of GMP.
	www.chm.bris.ac.uk /webprojects2003/rogers/998/Rhoeye.htm (684 words)

	InterPro: IPR000732 Rhodopsin
		The photoreceptor rhodopsin is a complex of the vision protein opsin and the chromophore 11-cis-retinal (derived from vitamin A) [ 1 ].
		Upon exposure to light, the 11-cis-retinal attached to rod or cone opsin isomerises to all-trans-retinal, which leads to the activation of the G protein transducin, and ultimately to the hyperpolarisation of the cell and the propagation of a nerve impulse that is perceived as light.
		Fryxell K.J. Meyerowitz E.M. The evolution of rhodopsins and neurotransmitter receptors.
	www.ebi.ac.uk /interpro/IEntry?ac=IPR000732 (3058 words)

	Mutant rab8 Impairs Docking and Fusion of Rhodopsin-bearing Post-Golgi Membranes and Causes Cell Death of Transgenic ...
		of rhodopsin and cause retinitis pigmentosa (Berson 1993
		Rhodopsin is synthesized within the IS and transported on membranes that bud from the TGN and fuse with the plasma membrane
		Rab11 mediates post-Golgi trafficking of rhodopsin to the photosensitive apical membrane of Drosophila photoreceptors
	www.molbiolcell.org /cgi/content/full/12/8/2341 (6316 words)

	RHODOPSIN AS A CHEMICAL COMPLEX OF RHODONINE AND OPSIN
		To appreciate the precise concept of rhodopsin as a complex based on the experiments provided in the literature, it is first necessary to review a number of simpler concepts and facts.
		Rhodopsin as defined above is a chemical complex of Rhodonine and opsin that is non-functional in the absence of a de-excitation mechanism (the dendrites) and the associated electrical power source (the glutamate-based electrostenolytic mechanism) Both the dendrites and the electrostenolytic mechanism depend on the electrical conductivity of the IPM.
		The relatively crude chemical laboratory techniques used in the 1930-60's were not compatible with the study of the rhodopsin complex or the recovery of the chromophores of vision.
	www.4colorvision.com /files/rhodopsin.htm (2657 words)

	Rho - rhodopsin
		Light-dependent rhodopsin phosphorylation and dephosphorylation are also normal or nearly normal as determined by (i) immunostaining of PPEF-2-/- retinas with the phosphorhodopsin-specific antibody RT-97 and (ii) mass spectrometry of C-terminal rhodopsin peptides from mice lacking both PPEF-1 and PPEF-2.
		Because GRK1 (rhodopsin kinase), the GRK that mediates rhodopsin desensitization in the rod cell, is reportedly expressed in both rods and cones, a detailed comparison of the localization of the two kinases is a necessary step toward determining their potential roles in cone visual signaling.
		The transcription factor AP-1, a central element in the apoptotic response to light, is not activated in the absence of rhodopsin, indicating that rhodopsin is essential for the generation or transduction of the intracellular death signal induced by light.
	www.ihop-net.org /UniPub/iHOP/gg/151712.html (6721 words)

	BioCarta - Charting Pathways of Life (Site not responding. Last check: 2007-10-29)
		Rhodopsin in the discs of rod cells contains a bound 11-cis retinal chromophore, a small molecule derived from Vitamin A that acts as the light sensitive portion of the receptor molecule, absorbing light to initiate the signal transduction cascade.
		This change in rhodopsin’s shape alters its interaction with transducin, the member of the G-protein gene family that is specific in its role in visual signal transduction.
		Dissociation and reassociation of retinal, dephosphorylation of rhodopsin and release of arrestin all return rhodopsin to its ready state, prepared once again to respond to light.
	www.biocarta.com /pathfiles/h_rhodopsinPathway.asp (447 words)

	Rhodopsin Transport (Site not responding. Last check: 2007-10-29)
		The cells at the far edge of the image at right lack a transporter required for rhodopsin trafficking, hence the rhabdomeres are small.
		In humans, the most common type of dominantly inherited retinitis pigmentosa disease is due to missense mutations in rhodopsin.
		Currently, we are using molecular and genetic approaches to define the cellular role of the identified genes.
	www.nd.edu /~jotousa/labwww/Pages/RhoTransport.html (120 words)

	The Rhodopsin Cycle
		Rhodopsin undergoes a cyclic decomposition and reconstitution in response to the presence of light.
		The disintegration of rhodopsin into retinal and scotopsin is progressive, with a series of short-lived intermediate compounds formed, as shown in the diagram to the right.
		The cascade is reversed by the presence of rhodopsin kinase, another enzyme present in the rod outer segment, and the sodium channels are re-opened.
	education.vetmed.vt.edu /Curriculum/VM8054/EYE/RHODOPSN.HTM (793 words)

	Molecular Dynamics Study of Rhodopsin
		At the beginning of the visual process is the 7-transmembrane protein rhodopsin.
		In case of rhodopsin the ligand retinal is covalently bound to receptor and works an inverse agonist locking the protein in the quiescent state.
		We have studied the effects of the cis-trans isomerization of retinal on the conformation of the protein using molecular dynamics simulations.
	www.ks.uiuc.edu /Research/rhodopsin (400 words)

	Structural and functional impairment of endocytic pathways by retinitis pigmentosa mutant rhodopsin-arrestin complexes ...
		Rhodopsin immunoreactivity colocalized with the internalized Tf or dextran is marked by arrows, and merge images are shown in E, H, and K.
		Rhodopsin expressed in tissue culture is heterogeneously glycosylated and prone to forming higher-order aggregates (2, 5), which accounts for the broadened bands on SDS-PAGE.
		Rhodopsin arginine-135 mutants are phosphorylated by rhodopsin kinase and bind arrestin in the absence of 11-cis-retinal.
	www.jci.org /cgi/content/full/114/1/131 (6220 words)

	Retina International's Scientific Newsletter - Rhodopsin Mutations
		Antinolo,G., Sanchez,B., Borrego,S., Rueda,T., Chaparro,P., and Cabeza,J.C. Identification of a new mutation at codon 171 of rhodopsin gene causing autosomal dominant retinitis pigmentosa.
		Gal,A., Artlich,A., Ludwig,M., Niemeyer,G., Olek,K., Schwinger,E., and Schinzel,A. Pro-347-Arg mutation of the rhodopsin gene in autosomal dominant retinitis pigmentosa.
		Hwa,J., Garriga,P., Liu,X., and Khorana,H.G. Structure and function in rhodopsin: packing of the helices in the transmembrane domain and folding to a tertiary structure in the intradiscal domain are coupled.
	www.retina-international.org /sci-news/rhomut.htm (1562 words)

	How We See: The First Steps of Human Vision
		It is the rhodopsin protein in the retina that absorbs the light that enters the eye.
		Since rhodopsin's function is to absorb light it is not surprising that scientists should use light to elucidate the behavior of the molecule.
		The authors identified a portion of the rhodopsin that was required for binding and aiding in the formation of the neural signal.
	www.accessexcellence.org /AE/AEC/CC/vision_background.html (2916 words)

	Normal Light Response, Photoreceptor Integrity, and Rhodopsin Dephosphorylation in Mice Lacking Both Protein ...
		The phosphorylation state of rhodopsin was measured 3, 30, and 120 min following a flash of light that bleached roughly 20% of the rhodopsin in the eye in wild-type (left side) and 2×KO mice (right side).
		Inactivation of photoexcited rhodopsin in retinal rods: the roles of rhodopsin kinase and 48-kDa protein (arrestin).
		A rhodopsin gene mutation responsible for autosomal dominant retinitis pigmentosa results in a protein that is defective in localization to the photoreceptor outer segment.
	mcb.asm.org /cgi/content/full/21/24/8605 (5468 words)

	Regulation of Rhodopsin Gene Expression
		Preliminary transgenic mouse studies with fusion construct sconsisting of sequences upstream of the bovine rhodopsin gene ligated to the reporter gene lacZ (beta-galactosidase) have identified cis-acting DNA regulatory sequences that are capable of directing photoreceptor cell-specific gene expression.
		DNA sequence comparisons of rhodopsin upstream regions from different species and in vitro DNA-protein binding studies (work for which funding is not being requested in this application) will be used to aid in the decision of which additional constructs to make.
		Due to the time and expense involved in transgenic studies, efforts will also be made to complement the transgenic studies with simpler methods for the in vivo study of retinal cis-acting elements.
	www.hopkinsmedicine.org /wilmer/research/glaurhod.html (456 words)

	Identification of an Outer Segment Targeting Signal in the COOH Terminus of Rhodopsin Using Transgenic Xenopus laevis ...
		Trafficking of Endogenous Rhodopsin Is Not Disrupted in Transgenic Photoreceptors
		Likewise, GFP-CT44del25 (A 3) is abundant in the synaptic terminal; rhodopsin (B 3) is not.
		Jules, R.S., and O'Brien, P.J. The acylation of rat rhodopsin in vitro and in vivo.
	www.jcb.org /cgi/content/full/151/7/1369 (6856 words)

	Effect of Packing Density on Rhodopsin Stability and Function in Polyunsaturated Membranes -- Niu and Mitchell 89 (3): ...
		of rhodopsin is manifested by the increase of the denaturation
		Light-induced phosphorylation of rhodopsin in cattle photoreceptor membranes: substrate activation and inactivation.
		Thermal destabilization of rhodopsin and opsin by proteolytic cleavage in bovine rod outer segment disk membranes.
	www.biophysj.org /cgi/content/full/89/3/1833 (3705 words)

	Rhodopsin C terminus, the site of mutations causing retinal disease, regulates trafficking by binding to ...
		The rhodopsin C-terminal peptide and the GST fusion protein containing the C terminus of rhodopsin specifically bind a 20-kDa protein, a member of the ARF family of small GTPases.
		(B) Sequence of the frog rhodopsin C-terminal peptide (peptide C) folded as predicted from the crystal structure of rhodopsin (29).
		The mutations in the C-terminal region of rhodopsin that cause
	www.pnas.org /cgi/content/full/102/9/3301 (4589 words)

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