ArticlePNAS nexus2023
Allosteric modulation of integral protein activity by differential stress in asymmetric membranes.
Article in PNAS nexus, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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.
The trial behind it
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
10 citing papers in PubMed, 19 citations in OpenAlex.
- Inside the membrane: a closer look using elastic scattering techniques and friends.European biophysics journal : EBJ · 2026Review
- The lateral stress profile of fluid lipid membranes as revealed by the diffuse interface approach.Biophysical journal · 2025Article
- Allosteric coupling between a lipid bilayer and a membrane protein.Biophysical journal · 2025Article
- The membrane properties determine protein function: A new aspect of allosteric modulation.Biophysical journal · 2025Article
- Elucidating the mechanical properties of asymmetric membranes by direct derivation of their energetics.Faraday discussions · 2025Article
- Metal ion cofactors modulate integral enzyme activity by varying differential membrane curvature stress.RSC applied interfaces · 2025Article
- Evaluating the impact of the membrane thickness on the function of the intramembrane protease GlpG.Biophysical journal · 2024Article
- Substrate specificity controlled by the exit site of human P4-ATPases, revealed by de novo point mutations in neurological disorders.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Methyl-β-cyclodextrin asymmetrically extracts phospholipid from bilayers, granting tunable control over differential stress in lipid vesicles.Soft matter · 2024Article
- The asymmetric plasma membrane-A composite material combining different functionalities?: Balancing Barrier Function and Fluidity for Effective Signaling.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The activity of integral membrane proteins is tightly coupled to the properties of the surrounding lipid matrix. In particular, transbilayer asymmetry, a hallmark of all plasma membranes, might be exploited to control membrane-protein activity. Here, we hypothesized that the membrane-embedded enzyme outer membrane phospholipase A (OmpLA) is susceptible to the lateral pressure differences that build up between such asymmetric membrane leaflets. Upon reconstituting OmpLA into synthetic, chemically well-defined phospholipid bilayers exhibiting different lateral pressure profiles, we indeed observed a substantial decrease in the enzyme's hydrolytic activity with increasing membrane asymmetry. No such effects were observed in symmetric mixtures of the same lipids. To quantitatively rationalize how the differential stress in asymmetric lipid bilayers inhibits OmpLA, we developed a simple allosteric model within the lateral pressure framework. Thus, we find that membrane asymmetry can serve as the dominant factor in controlling membrane-protein activity, even in the absence of specific, chemical cues or other physical membrane determinants such as hydrophobic mismatch.
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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 Socratic graph.