Journal
JOURNAL OF CELL BIOLOGY
Volume 220, Issue 8, Pages -Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.202101063
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Categories
Funding
- Visual Science Research Core of Case Western Reserve University (Cleveland, OH) [P30 EY11373]
- National Institutes of Health (NIH) [EY009339, EY027283, EY030873, EY019312]
- U.S. Department of Veterans Affairs [I01BX004939]
- Thome Memorial Foundation Program in Age-Related Macular Degeneration Research
- National Eye Institute [T32EY007157-17, T32EY007157-16A1]
- Research to Prevent Blindness
- Department of Ophthalmology, University of California, Irvine
- Mass Spectrometry Core of the Salk Institute
- NIH National Cancer Institute Cancer Center Support Grant [P30 014195]
- Helmsley Center for Genomic Medicine
- National Institutes of Health [1S10OD021815-01, P41-GM103311]
- [T32GM007250]
- [T32GM008803]
- [F30EY029136-01A1]
- [T32EY024236]
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The study revealed differences in lipid composition between the central and rim regions of photoreceptor ROS, highlighting potential protein-lipid interactions. High-resolution profiling of ROS disk lipid composition provides insights into the balance of intricate membrane structure and protein activity within the ROS, serving as a model for future studies of complex cellular structures.
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.
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