ArticleBiophysical journal2004
Cholesterol modulates the organization of the gammaM4 transmembrane domain of the muscle nicotinic acetylcholine receptor.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 47 citations in OpenAlex.
- Quantifying Small-Molecule Association with Lipid Membranes: Methods, Models, and Limitations.Membranes · 2026Review
- Physics-based evolution of transmembrane helices reveals mechanisms of cholesterol attraction.Nature communications · 2025Article
- Fluorescence Studies of Nicotinic Acetylcholine Receptor and Its Associated Lipid Milieu: The Influence of Erwin London's Methodological Approaches.The Journal of membrane biology · 2022Review
- Pathways and Mechanisms of Cellular Cholesterol Efflux-Insight From Imaging.Frontiers in cell and developmental biology · 2022Review
- Fluorescence microscopy imaging of a neurotransmitter receptor and its cell membrane lipid milieu.Frontiers in molecular biosciences · 2022Review
- Transmembrane Domain Dissociation Is Required for Hendra Virus F Protein Fusogenic Activity.Journal of virology · 2019Article
- Site-Directed Fluorescence Approaches for Dynamic Structural Biology of Membrane Peptides and Proteins.Frontiers in molecular biosciences · 2019Review
- Alzheimer's Disease as a Membrane Disorder: Spatial Cross-Talk Among Beta-Amyloid Peptides, Nicotinic Acetylcholine Receptors and Lipid Rafts.Frontiers in cellular neuroscience · 2019Review
- A mirror code for protein-cholesterol interactions in the two leaflets of biological membranes.Scientific reports · 2016Article
- Organization and dynamics of SNARE proteins in the presynaptic membrane.Frontiers in physiology · 2015Review
- Organization and dynamics of Fas transmembrane domain in raft membranes and modulation by ceramide.Biophysical journal · 2011Article
- Disclosure of cholesterol recognition motifs in transmembrane domains of the human nicotinic acetylcholine receptor.Scientific reports · 2011Article
- Molecular simulation of the effect of cholesterol on lipid-mediated protein-protein interactions.Biophysical journal · 2010Article
- Partition profile of the nicotinic acetylcholine receptor in lipid domains upon reconstitution.Journal of lipid research · 2010Article
- Membrane microheterogeneity: Förster resonance energy transfer characterization of lateral membrane domains.European biophysics journal : EBJ · 2010Review
- Is there a preferential interaction between cholesterol and tryptophan residues in membrane proteins?Biochemistry · 2008Article
- Plasma membrane sterol distribution resembles the surface topography of living cells.Molecular biology of the cell · 2007Article
- Distinct gamma2 subunit domains mediate clustering and synaptic function of postsynaptic GABAA receptors and gephyrin.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2005Article
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Authors and funding
6 authors at 4 institutions in 3 countries.
Funding
Abstract
A 28-mer gammaM4 peptide, obtained by solid-state synthesis and corresponding to the fourth transmembrane segment of the nicotinic acetylcholine receptor gamma-subunit, possesses a single tryptophan residue (Trp453), making it an excellent model for studying peptide-lipid interactions in membranes by fluorescence spectroscopy. The gammaM4 peptide was reconstituted with synthetic lipids (vesicles of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine, i.e., POPC) rich and poor in cholesterol and analyzed using steady-state and time-resolved fluorescence techniques. The decrease in gammaM4 intrinsic fluorescence lifetime observed upon incorporation into a cholesterol-rich lo phase could be rationalized on the basis of a dynamic self-quenching owing to the formation of peptide-rich patches in the membrane. This agrees with the low Förster type resonance energy transfer efficiency from the Trp453 residue to the fluorescent cholesterol analog, dehydroergosterol, in the lo phase. In the absence of cholesterol the gammaM4 nicotinic acetylcholine receptor peptide is randomly distributed in the POPC bilayer with its hydrophobic moiety matching the membrane thickness, whereas in the presence of cholesterol the increase in the membrane thickness and variation of the material properties favor the formation of peptide-enriched patches, i.e., interhelix interaction energy is essential for obtaining a stabilized structure. Thus, the presence of a cholesterol-rich, ordered POPC phase drives the organization of peptide-enriched patches, in which the gammaM4 peptide occupies approximately 30% of the patch area.
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