Open AccessNano-scale resolution of native retinal rod disk membranes reveals differences in lipid composition
Author(s) -
Christian Sander,
Avery E. Sears,
Antônio Frederico Michel Pinto,
Elliot H. Choi,
Shirin Kahremany,
Fangyuan Gao,
David Salom,
Hui Jin,
Els Pardon,
Suk-Hwan Suh,
Zhiqian Dong,
Jan Steyaert,
Alan Saghatelian,
Dorota SkowronskaKrawczyk,
Philip D. Kiser,
Krzysztof Palczewski
Publication year - 2021
Publication title -
the journal of cell biology/the journal of cell biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.414
H-Index - 380
eISSN - 1540-8140
pISSN - 0021-9525
DOI - 10.1083/jcb.202101063
Subject(s) - rhodopsin , membrane , biophysics , biology , membrane lipids , phospholipid , biochemistry , chemistry , microbiology and biotechnology , membrane protein , high resolution , retinal , remote sensing , geology
Photoreceptors rely on distinct membrane compartments to support their specialized function. Unlike protein localization, identification of critical differences in membrane content has not yet been expanded to lipids, due to the difficulty of isolating domain-specific samples. We have overcome this by using SMA to coimmunopurify membrane proteins and their native lipids from two regions of photoreceptor ROS disks. Each sample's copurified lipids were subjected to untargeted lipidomic and fatty acid analysis. Extensive differences between center (rhodopsin) and rim (ABCA4 and PRPH2/ROM1) samples included a lower PC to PE ratio and increased LC- and VLC-PUFAs in the center relative to the rim region, which was enriched in shorter, saturated FAs. The comparatively few differences between the two rim samples likely reflect specific protein–lipid interactions. High-resolution profiling of the ROS disk lipid composition gives new insights into how intricate membrane structure and protein activity are balanced within the ROS, and provides a model for future studies of other complex cellular structures.