ArticleBiophysical journal2013
Transmembrane protein (perfringolysin o) association with ordered membrane domains (rafts) depends upon the raft-associating properties of protein-bound sterol.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 20 citations in OpenAlex.
- Mimicking effects of cholesterol in lipid bilayer membranes by self-assembled amphiphilic block copolymers.Soft matter · 2023Article
- A basic model for the association of ligands with membrane cholesterol: application to cytolysin binding.Journal of lipid research · 2023Article
- A palmitoylation code controls PI4KIIIα complex formation and PI(4,5)P2 homeostasis at the plasma membrane.Journal of cell science · 2022Article
- Preparation and utility of asymmetric lipid vesicles for studies of perfringolysin O-lipid interactions.Methods in enzymology · 2021Article
- Peripheral myelin protein 22 preferentially partitions into ordered phase membrane domains.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Proteomic Analysis of Lipid Rafts from RBL-2H3 Mast Cells.International journal of molecular sciences · 2019Article
- Effect of sterol structure on ordered membrane domain (raft) stability in symmetric and asymmetric vesicles.Biochimica et biophysica acta. Biomembranes · 2019Article
- Article
- Effects of host cell sterol composition upon internalization ofThe Journal of biological chemistry · 2018Article
- The effect of sterol structure upon clathrin-mediated and clathrin-independent endocytosis.Journal of cell science · 2017Article
- Ordered Membrane Domain-Forming Properties of the Lipids of Borrelia burgdorferi.Biophysical journal · 2016Article
- Review
- Raft-like membrane domains in pathogenic microorganisms.Current topics in membranes · 2015Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Because transmembrane (TM) protein localization, or nonlocalization, in ordered membrane domains (rafts) is a key to understanding membrane domain function, it is important to define the origin of protein-raft interaction. One hypothesis is that a tight noncovalent attachment of TM proteins to lipids that have a strong affinity for ordered domains can be sufficient to induce raft-protein interaction. The sterol-binding protein perfringolysin O (PFO) was used to test this hypothesis. PFO binds both to sterols that tend to localize in ordered domains (e.g., cholesterol), and to those that do not (e.g., coprostanol), but it does not bind to epicholesterol, a raft-promoting 3α-OH sterol. Using a fluorescence resonance energy transfer assay in model membrane vesicles containing coexisting ordered and disordered lipid domains, both TM and non-TM forms of PFO were found to concentrate in ordered domains in vesicles containing high and low-Tm lipids plus cholesterol or 1:1 (mol/mol) cholesterol/epicholesterol, whereas they concentrate in disordered domains in vesicles containing high-Tm and low-Tm lipids plus 1:1 (mol/mol) coprostanol/epicholesterol. Combined with previous studies this behavior indicates that TM protein association with ordered domains is dependent upon both the association of the protein-bound sterol with ordered domains and hydrophobic match between TM segments and rafts.
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