Evidence map›Paper›PMID 30954213›Full record

ArticleBiophysical journal2019

Phosphatidylserine Asymmetry Promotes the Membrane Insertion of a Transmembrane Helix.

Haden L Scott, Frederick A Heberle, John Katsaras, Francisco N Barrera

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.7field-weighted citation impact, top 15% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

27 citing papers in PubMed, 51 citations in OpenAlex.

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  14. Arginine Residues Modulate the Membrane Interactions of pHLIP Peptides.Journal of chemical information and modeling · 2023
    Article
  15. Review
  16. Review
  17. pHLIP Peptides Target Acidity in Activated Macrophages.Molecular imaging and biology · 2022
    Article
  18. CaProtein science : a publication of the Protein Society · 2022
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 3 institutions in 2 countries.

Haden L ScottDepartment of Biochemistry & Cellular and Molecular Biology, University of Tennessee, Knoxville, Tennessee.
Frederick A HeberleThe Bredesen Center for Interdisciplinary Research and Graduate Education, University of Tennessee, Knoxville, Tennessee; Shull Wollan Center-a Joint Institute for Neutron Sciences, Oak Ridge, Tennessee.
John KatsarasDepartment of Physics and Astronomy, University of Tennessee, Knoxville, Tennessee; Shull Wollan Center-a Joint Institute for Neutron Sciences, Oak Ridge, Tennessee; Large Scale Structures Group, Neutron Sciences Directorate, Oak Ridge National Laboratory, Oak Ridge, Tennessee; Department of Physics, Brock University, St. Catharines, Ontario, Canada.
Francisco N BarreraDepartment of Biochemistry & Cellular and Molecular Biology, University of Tennessee, Knoxville, Tennessee. Electronic address: fbarrera@utk.edu.
University of Tennessee at Knoxville · USJoint Institute for Computational Sciences · USOak Ridge National Laboratory · US

Funding

Transmembrane Peptides for Targeting Acidosis - Equipment SupplementR01GM120642 · NIGMS · UNIVERSITY OF TENNESSEE KNOXVILLE · PI BARRERA, FRANCISCO NICOLAS · 2016 to 2020
$1.7M
NIGMS NIH HHS R01 GM120642
6 · The paper itself

Abstract

The plasma membrane (PM) contains an asymmetric distribution of lipids between the inner and outer bilayer leaflets. A lipid of special interest in eukaryotic membranes is the negatively charged phosphatidylserine (PS). In healthy cells, PS is actively sequestered to the inner leaflet of the PM, but PS redistributes to the outer leaflet when the cell is damaged or at the onset of apoptosis. However, the influence of PS asymmetry on membrane protein structure and folding are poorly understood. The pH low insertion peptide (pHLIP) adsorbs to the membrane surface at a neutral pH, but it inserts into the membrane at an acidic pH. We have previously observed that in symmetric vesicles, PS affects the membrane insertion of pHLIP by lowering the pH midpoint of insertion. Here, we studied the effect of PS asymmetry on the membrane interaction of pHLIP. We developed a modified protocol to create asymmetric vesicles containing PS and employed Annexin V labeled with an Alexa Fluor 568 fluorophore as a new probe to quantify PS asymmetry. We observed that the membrane insertion of pHLIP was promoted by the asymmetric distribution of negatively charged PS, which causes a surface charge difference between bilayer leaflets. Our results indicate that lipid asymmetry can modulate the formation of an α-helix on the membrane. A corollary is that model studies using symmetric bilayers to mimic the PM may fail to capture important aspects of protein-membrane interactions.

Indexed as

Amino Acid SequenceHydrogen-Ion ConcentrationHydrophobic and Hydrophilic InteractionsLipid BilayersMembrane ProteinsModels, ChemicalPhosphatidylserinesPhosphorylcholineProtein ConformationStructure-Activity RelationshipLipid BilayersMembrane ProteinspHLIP proteinPhosphatidylserinesPhosphorylcholine

Identifiers

PMID30954213
PMCPMC6486527
OpenAlexW2925222378

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.