Evidence map›Paper›PMID 25897971›Full record

ArticleNature communications2015

GPI-anchored proteins do not reside in ordered domains in the live cell plasma membrane.

Eva Sevcsik, Mario Brameshuber, Martin Fölser, Julian Weghuber, Alf Honigmann, Gerhard J Schütz

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
9.2field-weighted citation impact, top 1% 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

64 citing papers in PubMed, 126 citations in OpenAlex.

  1. Review
  2. Article
  3. A novel transgenic reporter of extracellular acidification in zebrafish elucidates skeletal muscle T-tubule pH regulation.Developmental dynamics : an official publication of the American Association of Anatomists · 2025
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  5. Review
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  9. Review
  10. Role of the membrane anchor in the regulation of Lck activity.The Journal of biological chemistry · 2022
    Article
  11. Article
  12. Article
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  15. Article
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  17. Article
  18. Critical Phenomena in Plasma Membrane Organization and Function.Annual review of physical chemistry · 2021
    Review
  19. Zwitterionic Character and Lipid Composition Determine the Behaviour of Glycosylphosphatidylinositol Fragments in Monolayers.Chemphyschem : a European journal of chemical physics and physical chemistry · 2021
    Article
  20. Article

4 more citing papers are in PubMed but not listed here.

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

6 authors at 3 institutions in 2 countries.

Eva SevcsikInstitute of Applied Physics, Vienna University of Technology, Wiedner Hauptstrasse 8-10, Vienna 1040, Austria.
Mario BrameshuberInstitute of Applied Physics, Vienna University of Technology, Wiedner Hauptstrasse 8-10, Vienna 1040, Austria.
Martin FölserInstitute of Applied Physics, Vienna University of Technology, Wiedner Hauptstrasse 8-10, Vienna 1040, Austria.
Julian WeghuberSchool of Engineering and Environmental Sciences, University of Applied Sciences Upper Austria, Stelzhamerstrasse 23, Wels 4600, Austria.
Alf HonigmannDepartment of NanoBiophotonics, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, Göttingen 37077, Germany.
Gerhard J SchützInstitute of Applied Physics, Vienna University of Technology, Wiedner Hauptstrasse 8-10, Vienna 1040, Austria.
TU Wien · ATMax Planck Society · DEUniversity of Applied Sciences Upper Austria · AT

Funding

Austrian Science Fund FWF P 25730Austrian Science Fund FWF P 26337
6 · The paper itself

Abstract

The organization of proteins and lipids in the plasma membrane has been the subject of a long-lasting debate. Membrane rafts of higher lipid chain order were proposed to mediate protein interactions, but have thus far not been directly observed. Here we use protein micropatterning combined with single-molecule tracking to put current models to the test: we rearranged lipid-anchored raft proteins (glycosylphosphatidylinositol(GPI)-anchored-mGFP) directly in the live cell plasma membrane and measured the effect on the local membrane environment. Intriguingly, this treatment does neither nucleate the formation of an ordered membrane phase nor result in any enrichment of nanoscopic-ordered domains within the micropatterned regions. In contrast, we find that immobilized mGFP-GPIs behave as inert obstacles to the diffusion of other membrane constituents without influencing their membrane environment over distances beyond their physical size. Our results indicate that phase partitioning is not a fundamental element of protein organization in the plasma membrane.

Indexed as

CarcinomaCD59 AntigensCell Line, TumorCell MembraneGlycosylphosphatidylinositolsGreen Fluorescent ProteinsHumansImmunoglobulin Fab FragmentsLipid-Linked ProteinsProtein Structure, TertiaryCD59 AntigensGlycosylphosphatidylinositolsGreen Fluorescent ProteinsImmunoglobulin Fab FragmentsLipid-Linked Proteins

Identifiers

PMID25897971
PMCPMC4430820
OpenAlexW2024692900

What OpenQuestion holds

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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.