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PLoS One
2015 Oct 20;1010:e0141114. doi: 10.1371/journal.pone.0141114.
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Rhodopsin Forms Nanodomains in Rod Outer Segment Disc Membranes of the Cold-Blooded Xenopus laevis.
Rakshit T
,
Senapati S
,
Sinha S
,
Whited AM
,
Park PS
.
???displayArticle.abstract??? Rhodopsin forms nanoscale domains (i.e., nanodomains) in rod outer segment disc membranes from mammalian species. It is unclear whether rhodopsin arranges in a similar manner in amphibian species, which are often used as a model system to investigate the function of rhodopsin and the structure of photoreceptor cells. Moreover, since samples are routinely prepared at low temperatures, it is unclear whether lipid phase separation effects in the membrane promote the observed nanodomain organization of rhodopsin from mammalian species. Rod outer segment disc membranes prepared from the cold-blooded frog Xenopus laevis were investigated by atomic force microscopy to visualize the organization of rhodopsin in the absence of lipid phase separation effects. Atomic force microscopy revealed that rhodopsin nanodomains form similarly as that observed previously in mammalian membranes. Formation of nanodomains in ROS disc membranes is independent of lipid phase separation and conserved among vertebrates.
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Fig 1. AFM image of an intact murine ROS disc. (A, B) Height (A) and deflection (B) images obtained by contact mode AFM generated using low force. (C, D) Height (C) and deflection (D) images obtained by contact mode AFM generated using higher force. The rim region (1) and nanodomains in the lamellar region (2) are discernible. Height images were scaled to a height range of 38 nm. Scale bar, 250 nm. Illustrations of a disc adsorbed on mica scanned by the AFM tip at low and high forces are shown next to AFM images. (E) A height profile is shown for the cross-section highlighted by a dotted line in panel C.
Fig 2. Murine ROS disc membranes imaged at 37°C. Representative images obtained by tapping mode AFM are shown. Murine ROS disc membranes were prepared at 4°C and imaged at 37°C. Height (left) and amplitude (right) images are shown. Height images were scaled to a height range of 25 nm. Scale bar, 500 nm.
Fig 3. X. laevis ROS disc membrane preparation. (A) The secondary structure of rhodopsin is shown with amino acid residue differences in X. laevis (red) and murine (blue) rhodopsin highlighted. (B) Light microscopy image of purified ROS from the retina of X. laevis. Scale bar, 15 μm. (C) SDS-PAGE of X. laevis (lane 1) and murine (lane 2) ROS disc membrane preparations. The sizes of protein standards are indicated in kDa.
Fig 4. AFM images of X. laevis ROS disc membranes. (A-G) Representative deflection images of X. laevis ROS disc membranes obtained by contact mode AFM. ROS disc membranes exhibit a varying number of lobes, which are formed by deeply penetrating incisures. Scale bar, 500 nm. (H) Histogram of nanodomain sizes measured in 57 images of X. laevis ROS disc membranes. The data was fit by a Log Gaussian function (n = 14,390).
Baylor,
Responses of retinal rods to single photons.
1979, Pubmed
Baylor,
Responses of retinal rods to single photons.
1979,
Pubmed
Bownds,
Light-sensitive swelling of isolated frog rod outer segments as an in vitro assay for visual transduction and dark adaptation.
1975,
Pubmed
Buzhynskyy,
Rhodopsin is spatially heterogeneously distributed in rod outer segment disk membranes.
2011,
Pubmed
Chabre,
X-ray diffraction studies of retinal rods. I. Structure of the disc membrane, effect of illumination.
1975,
Pubmed
Chabre,
Biophysics: is rhodopsin dimeric in native retinal rods?
2003,
Pubmed
Dell'Orco,
A physiological role for the supramolecular organization of rhodopsin and transducin in rod photoreceptors.
2013,
Pubmed
Engel,
Structure and mechanics of membrane proteins.
2008,
Pubmed
Fotiadis,
The G protein-coupled receptor rhodopsin in the native membrane.
2004,
Pubmed
Fotiadis,
Atomic-force microscopy: Rhodopsin dimers in native disc membranes.
2003,
Pubmed
Gunkel,
Higher-order architecture of rhodopsin in intact photoreceptors and its implication for phototransduction kinetics.
2015,
Pubmed
Haeri,
Rhodopsin mutant P23H destabilizes rod photoreceptor disk membranes.
2012,
Pubmed
,
Xenbase
Hamm,
Protein complement of rod outer segments of frog retina.
1986,
Pubmed
Heck,
Maximal rate and nucleotide dependence of rhodopsin-catalyzed transducin activation: initial rate analysis based on a double displacement mechanism.
2001,
Pubmed
Jin,
Opsin activation as a cause of congenital night blindness.
2003,
Pubmed
,
Xenbase
Kawamura,
Conservation of molecular interactions stabilizing bovine and mouse rhodopsin.
2010,
Pubmed
Kirchhoff,
Diffusion of molecules and macromolecules in thylakoid membranes.
2014,
Pubmed
Korenbrot,
Dark ionic flux and the effects of light in isolated rod outer segments.
1972,
Pubmed
Kwok-Keung Fung,
Photolyzed rhodopsin catalyzes the exchange of GTP for bound GDP in retinal rod outer segments.
1980,
Pubmed
Lamba,
Fourier transform infrared study of the rod outer segment disk and plasma membranes of vertebrate retina.
1994,
Pubmed
Liang,
Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes.
2003,
Pubmed
Liang,
Rhodopsin signaling and organization in heterozygote rhodopsin knockout mice.
2004,
Pubmed
Liebman,
Visual pigments of frog and tadpole (Rana pipiens).
1968,
Pubmed
Lodowski,
Signals governing the trafficking and mistrafficking of a ciliary GPCR, rhodopsin.
2013,
Pubmed
,
Xenbase
Mazelova,
Ciliary targeting motif VxPx directs assembly of a trafficking module through Arf4.
2009,
Pubmed
,
Xenbase
Molday,
Peripherin. A rim-specific membrane protein of rod outer segment discs.
1987,
Pubmed
Muller,
AFM: a nanotool in membrane biology.
2008,
Pubmed
Najafi,
Impact of signaling microcompartment geometry on GPCR dynamics in live retinal photoreceptors.
2012,
Pubmed
,
Xenbase
Nickell,
Three-dimensional architecture of murine rod outer segments determined by cryoelectron tomography.
2007,
Pubmed
NILSSON,
THE ULTRASTRUCTURE OF THE RECEPTOR OUTER SEGMENTS IN THE RETINA OF THE LEOPARD FROG (RANA PIPIENS).
1965,
Pubmed
Papermaster,
Immunocytochemical localization of a large intrinsic membrane protein to the incisures and margins of frog rod outer segment disks.
1978,
Pubmed
Papermaster,
Rhodopsin content in the outer segment membranes of bovine and frog retinal rods.
1974,
Pubmed
Park,
Dynamic single-molecule force spectroscopy of rhodopsin in native membranes.
2015,
Pubmed
Rakshit,
Impact of reduced rhodopsin expression on the structure of rod outer segment disc membranes.
2015,
Pubmed
Rosenkranz,
New aspects of the ultrastructure of frog rod outer segments.
1977,
Pubmed
Tam,
Characterization of rhodopsin P23H-induced retinal degeneration in a Xenopus laevis model of retinitis pigmentosa.
2006,
Pubmed
,
Xenbase
Tam,
Identification of an outer segment targeting signal in the COOH terminus of rhodopsin using transgenic Xenopus laevis.
2000,
Pubmed
,
Xenbase
Tanuj Sapra,
Detecting molecular interactions that stabilize native bovine rhodopsin.
2006,
Pubmed
Teller,
Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs).
2001,
Pubmed
Tsukamoto,
The number, depth and elongation of disc incisures in the retinal rod of Rana catesbeiana.
1987,
Pubmed
Whited,
Atomic force microscopy: a multifaceted tool to study membrane proteins and their interactions with ligands.
2014,
Pubmed
Whited,
Nanodomain organization of rhodopsin in native human and murine rod outer segment disc membranes.
2015,
Pubmed
