ArticleThe EMBO journal2002
Topology of polytopic membrane protein subdomains is dictated by membrane phospholipid composition.
Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
51 citing papers in PubMed, 110 citations in OpenAlex.
- Lipochaperoning folding of water-soluble functional membrane protein in genetically and biosynthetically tuned EscherichiaiScience · 2026Article
- Single Molecule Force Spectroscopy to Probe Intermediates and Energetics of Membrane Protein Folding.Chemical reviews · 2026Review
- Its own architect: Flipping cardiolipin synthase.Science advances · 2025Article
- Structure and function ofProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Exploring Uniform, Dual, and Dynamic Topologies of Membrane Proteins by Substituted Cysteine Accessibility Method (SCAM™).Methods in molecular biology (Clifton, N.J.) · 2024Article
- Methods to study folding of alpha-helical membrane proteins in lipids.Open biology · 2022Review
- How bilayer properties influence membrane protein folding.Protein science : a publication of the Protein Society · 2020Review
- Cell-free expression tools to study co-translational folding of alpha helical membrane transporters.Scientific reports · 2020Article
- Structural and Functional Adaptability of Sucrose and Lactose Permeases fromBiochemistry · 2020Article
- The lipid-dependent structure and function of LacY can be recapitulated and analyzed in phospholipid-containing detergent micelles.Scientific reports · 2019Article
- Lipid-Assisted Membrane Protein Folding and Topogenesis.The protein journal · 2019Review
- Lipid-Dependent Alternating Access Mechanism of a Bacterial Multidrug ABC Exporter.ACS central science · 2019Article
- The folding, stability and function of lactose permease differ in their dependence on bilayer lipid composition.Scientific reports · 2017Article
- The Power of Asymmetry: Architecture and Assembly of the Gram-Negative Outer Membrane Lipid Bilayer.Annual review of microbiology · 2016Review
- Dynamic membrane protein topological switching upon changes in phospholipid environment.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Observing a lipid-dependent alteration in single lactose permeases.Structure (London, England : 1993) · 2015Article
- Lipids and topological rules governing membrane protein assembly.Biochimica et biophysica acta · 2014Review
- In vitro reconstitution of lipid-dependent dual topology and postassembly topological switching of a membrane protein.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- SAHBNET, an accessible surface-based elastic network: an application to membrane protein.International journal of molecular sciences · 2013Article
- A retrospective: use of Escherichia coli as a vehicle to study phospholipid synthesis and function.Biochimica et biophysica acta · 2013Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
In Escherichia coli, the major cytoplasmic domain (C6) of the polytopic membrane protein lactose permease (LacY) is exposed to the opposite side of the membrane from a neighboring periplasmic domain (P7). However, these domains are both exposed on the periplasmic side of the membrane in a mutant of E.coli lacking phosphatidylethanolamine (PE) wherein LacY only mediates facilitated transport. When purified LacY was reconstituted into liposomes lacking PE or phosphatidylcholine (PC), C6 and P7 were on the same side of the bilayer. In liposomes containing PE or PC, C6 and P7 were on opposite sides of the bilayer. Only the presence of PE in the liposomes restored active transport function of LacY as opposed to restoration of only facilitated transport function in the absence of PE. These results were the same for LacY purified from PE-containing or PE-lacking cells, and are consistent with the topology and function of LacY assembled in vivo. Therefore, irrespective of the mechanism of membrane insertion, the subdomain topological orientation and function of LacY are determined primarily by membrane phospholipid composition.
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Registered trials
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.