Rhodopsin Forms Nanodomains in Rod Outer Segment Disc Membranes of the Cold-Blooded Xenopus laevis.

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 ph...

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Main Authors: Tatini Rakshit, Subhadip Senapati, Satyabrata Sinha, A M Whited, Paul S-H Park
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2015-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC4619631?pdf=render
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spelling doaj-1780acdd43e245c2b33211d4f288483a2020-11-25T01:52:38ZengPublic Library of Science (PLoS)PLoS ONE1932-62032015-01-011010e014111410.1371/journal.pone.0141114Rhodopsin Forms Nanodomains in Rod Outer Segment Disc Membranes of the Cold-Blooded Xenopus laevis.Tatini RakshitSubhadip SenapatiSatyabrata SinhaA M WhitedPaul S-H ParkRhodopsin 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.http://europepmc.org/articles/PMC4619631?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Tatini Rakshit
Subhadip Senapati
Satyabrata Sinha
A M Whited
Paul S-H Park
spellingShingle Tatini Rakshit
Subhadip Senapati
Satyabrata Sinha
A M Whited
Paul S-H Park
Rhodopsin Forms Nanodomains in Rod Outer Segment Disc Membranes of the Cold-Blooded Xenopus laevis.
PLoS ONE
author_facet Tatini Rakshit
Subhadip Senapati
Satyabrata Sinha
A M Whited
Paul S-H Park
author_sort Tatini Rakshit
title Rhodopsin Forms Nanodomains in Rod Outer Segment Disc Membranes of the Cold-Blooded Xenopus laevis.
title_short Rhodopsin Forms Nanodomains in Rod Outer Segment Disc Membranes of the Cold-Blooded Xenopus laevis.
title_full Rhodopsin Forms Nanodomains in Rod Outer Segment Disc Membranes of the Cold-Blooded Xenopus laevis.
title_fullStr Rhodopsin Forms Nanodomains in Rod Outer Segment Disc Membranes of the Cold-Blooded Xenopus laevis.
title_full_unstemmed Rhodopsin Forms Nanodomains in Rod Outer Segment Disc Membranes of the Cold-Blooded Xenopus laevis.
title_sort rhodopsin forms nanodomains in rod outer segment disc membranes of the cold-blooded xenopus laevis.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2015-01-01
description 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.
url http://europepmc.org/articles/PMC4619631?pdf=render
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AT satyabratasinha rhodopsinformsnanodomainsinrodoutersegmentdiscmembranesofthecoldbloodedxenopuslaevis
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