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...
Main Authors: | , , , , |
---|---|
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 |
id |
doaj-1780acdd43e245c2b33211d4f288483a |
---|---|
record_format |
Article |
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 |
work_keys_str_mv |
AT tatinirakshit rhodopsinformsnanodomainsinrodoutersegmentdiscmembranesofthecoldbloodedxenopuslaevis AT subhadipsenapati rhodopsinformsnanodomainsinrodoutersegmentdiscmembranesofthecoldbloodedxenopuslaevis AT satyabratasinha rhodopsinformsnanodomainsinrodoutersegmentdiscmembranesofthecoldbloodedxenopuslaevis AT amwhited rhodopsinformsnanodomainsinrodoutersegmentdiscmembranesofthecoldbloodedxenopuslaevis AT paulshpark rhodopsinformsnanodomainsinrodoutersegmentdiscmembranesofthecoldbloodedxenopuslaevis |
_version_ |
1724994032541630464 |