ArticleJournal of lipid research2010
Partition profile of the nicotinic acetylcholine receptor in lipid domains upon reconstitution.
Article in Journal of lipid research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
15 citing papers in PubMed, 30 citations in OpenAlex.
- Five key challenges for the plasma membrane insertion of nicotinic acetylcholine receptors in cellular model systems.Molecular and cellular biochemistry · 2026Review
- Protein networking: nicotinic acetylcholine receptors and their protein-protein-associations.Molecular and cellular biochemistry · 2024Review
- Carlos Gutiérrez-Merino: Synergy of Theory and Experimentation in Biological Membrane Research.Molecules (Basel, Switzerland) · 2024Review
- Modulation of a rapid neurotransmitter receptor-ion channel by membrane lipids.Frontiers in cell and developmental biology · 2023Review
- 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
- A Role for Caveolin-3 in the Pathogenesis of Muscular Dystrophies.International journal of molecular sciences · 2020Review
- Untangling Direct and Domain-Mediated Interactions Between Nicotinic Acetylcholine Receptors in DHA-Rich Membranes.The Journal of membrane biology · 2019Article
- Boundary lipids of the nicotinic acetylcholine receptor: Spontaneous partitioning via coarse-grained molecular dynamics simulation.Biochimica et biophysica acta. Biomembranes · 2019Article
- 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
- Cholesterol modulates acetylcholine receptor diffusion by tuning confinement sojourns and nanocluster stability.Scientific reports · 2018Article
- Complex biomembrane mimetics on the sub-nanometer scale.Biophysical reviews · 2017Review
- Lateral pressure-mediated protein partitioning into liquid-ordered/liquid-disordered domains.Soft matter · 2016Article
- Cell-surface translational dynamics of nicotinic acetylcholine receptors.Frontiers in synaptic neuroscience · 2014Review
- Antibody-induced acetylcholine receptor clusters inhabit liquid-ordered and liquid-disordered domains.Biophysical journal · 2013Article
- Lipid rafts and Alzheimer's disease: protein-lipid interactions and perturbation of signaling.Frontiers in physiology · 2012Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nicotinic acetylcholine receptor (AChR) is in intimate contact with the lipids in its native membrane. Here we analyze the possibility that it is the intrinsic properties of the AChR that determine its partition into a given lipid domain. Torpedo AChR or a synthetic peptide corresponding to the AChR M4 segment (the one in closer contact with lipids) was reconstituted into "raft"-containing model membranes. The distribution of the AChR was assessed by Triton X-100 extraction in combination with fluorescence studies, and lipid analyses were performed on each sample. The influence of rapsyn, a peripheral protein involved in AChR aggregation, was studied. Raft-like domain aggregation was also studied using membranes containing the ganglioside GM1 followed by GM1 crosslinking. The gammaM4 peptide displays a marked preference for raft-like domains. In contrast, AChR alone or in the presence of rapsyn or ganglioside aggregation exhibits no such preference for raft-like domains, but it does cause a significant reduction in the total amount of these domains. The results indicate that the distribution of the AChR in lipid domains cannot be due exclusively to the intrinsic physicochemical properties of the protein and that there must be an external signal in native cell membranes that directs the AChR to a specific membrane domain.
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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.