ArticleProceedings of the National Academy of Sciences of the United States of America2014
Membrane raft association is a determinant of plasma membrane localization.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 113 papers.
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Who cites it
113 citing papers in PubMed, 221 citations in OpenAlex.
- Discovery and design of potent cell surface display elements.Nature biotechnology · 2026Article
- Visualizing suborganellar lipid distribution using correlative light and electron microscopy.Nature cell biology · 2026Article
- Palmitoylation of death receptor p75Alzheimer's research & therapy · 2026Article
- Apical and basolateral plasma membranes in epithelial cells have distinct lipidomes and biophysical properties.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Five key challenges for the plasma membrane insertion of nicotinic acetylcholine receptors in cellular model systems.Molecular and cellular biochemistry · 2026Review
- Transmembrane Domain Length of Influenza a Virus M2 Does Not Determine Its Non-Lipid Raft Localization.Viruses · 2026Article
- Membrane Composition Reshapes the Folding Landscape of a pH-Responsive Peptide.The journal of physical chemistry letters · 2026Article
- Visualizing dynamics of membrane rafts on live cells.Science advances · 2025Article
- ER exit sites mediated by the COPII adaptor sec24D selectively recruit lipid raft-preferring proteins for rapid ER export.Nature communications · 2025Article
- Apical and basolateral plasma membranes in epithelial cells have distinct lipidomes and biophysical properties.bioRxiv : the preprint server for biology · 2025Article
- Site-1 protease-mediated cholesterol metabolism is essential for lymphatic development in mice.JCI insight · 2025Article
- Article
- Microarray-Based Methodology for Lipid Profiling, Enzymatic Activity, And Binding Assays in Printed Lipid Raft Membranes from Astrocytes and Neurons.Analytical chemistry · 2025Article
- Diverse Interactions of Sterols with Amyloid Precursor Protein Transmembrane Domain Can Shift Distribution Between Alternative Amyloid-β Production Cascades in Manner Dependent on Local Lipid Environment.International journal of molecular sciences · 2025Article
- Flotillin-2 dampens T cell antigen sensitivity and functionality.JCI insight · 2024Article
- The transmembrane domain of the desmosomal cadherin desmoglein-1 governs lipid raft association to promote desmosome adhesive strength.Molecular biology of the cell · 2024Article
- Enhancing extracellular vesicle cargo loading and functional delivery by engineering protein-lipid interactions.Nature communications · 2024Article
- Article
- Dysregulation of cellular membrane homeostasis as a crucial modulator of cancer risk.The FEBS journal · 2024Review
- Sorting of secretory proteins at theeLife · 2024Article
53 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The lipid raft hypothesis proposes lateral domains driven by preferential interactions between sterols, sphingolipids, and specific proteins as a central mechanism for the regulation of membrane structure and function; however, experimental limitations in defining raft composition and properties have prevented unequivocal demonstration of their functional relevance. Here, we establish a quantitative, functional relationship between raft association and subcellular protein sorting. By systematic mutation of the transmembrane and juxtamembrane domains of a model transmembrane protein, linker for activation of T-cells (LAT), we generated a panel of variants possessing a range of raft affinities. These mutations revealed palmitoylation, transmembrane domain length, and transmembrane sequence to be critical determinants of membrane raft association. Moreover, plasma membrane (PM) localization was strictly dependent on raft partitioning across the entire panel of unrelated mutants, suggesting that raft association is necessary and sufficient for PM sorting of LAT. Abrogation of raft partitioning led to mistargeting to late endosomes/lysosomes because of a failure to recycle from early endosomes. These findings identify structural determinants of raft association and validate lipid-driven domain formation as a mechanism for endosomal protein sorting.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.