Evidence map›Paper›PMID 26038815›Full record

ArticleLangmuir : the ACS journal of surfaces and colloids2015

Formation of Giant Unilamellar Proteo-Liposomes by Osmotic Shock.

Isabelle Motta, Andrea Gohlke, Vladimir Adrien, Feng Li, Hélène Gardavot, James E Rothman, Frederic Pincet

Erratum issuedAbstract read
In one paragraph

Article in Langmuir : the ACS journal of surfaces and colloids, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
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

23 citing papers in PubMed.

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  7. SecYEG-mediated translocation in a model synthetic cell.Synthetic biology (Oxford, England) · 2024
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Isabelle Motta†Laboratoire de Physique Statistique, Ecole Normale Supérieure de Paris, Université Pierre et Marie Curie, Université Paris Diderot, Centre National de la Recherche Scientifique, UMR 8550, 24 rue Lhomond, 75005 Paris, France.
Andrea Gohlke†Laboratoire de Physique Statistique, Ecole Normale Supérieure de Paris, Université Pierre et Marie Curie, Université Paris Diderot, Centre National de la Recherche Scientifique, UMR 8550, 24 rue Lhomond, 75005 Paris, France.
Vladimir Adrien†Laboratoire de Physique Statistique, Ecole Normale Supérieure de Paris, Université Pierre et Marie Curie, Université Paris Diderot, Centre National de la Recherche Scientifique, UMR 8550, 24 rue Lhomond, 75005 Paris, France.
Feng Li‡Department of Cell Biology, Nanobiology Institute, School of Medicine, Yale University, 333 Cedar Street, New Haven, Connecticut 06520, United States.
Hélène Gardavot†Laboratoire de Physique Statistique, Ecole Normale Supérieure de Paris, Université Pierre et Marie Curie, Université Paris Diderot, Centre National de la Recherche Scientifique, UMR 8550, 24 rue Lhomond, 75005 Paris, France.
James E Rothman‡Department of Cell Biology, Nanobiology Institute, School of Medicine, Yale University, 333 Cedar Street, New Haven, Connecticut 06520, United States.
Frederic Pincet†Laboratoire de Physique Statistique, Ecole Normale Supérieure de Paris, Université Pierre et Marie Curie, Université Paris Diderot, Centre National de la Recherche Scientifique, UMR 8550, 24 rue Lhomond, 75005 Paris, France.

Funding

Regulation of Membrane Fusion in ExocytosisR01DK027044 · NIDDK · YALE UNIVERSITY · PI KRISHNAKUMAR, SHYAM S · 1986 to 2021
$8.2M
NIDDK NIH HHS R01 DK027044
6 · The paper itself

Abstract

Giant unilamellar vesicles (GUVs), composed of a phospholipid bilayer, are often used as a model system for cell membranes. However, the study of proteo-membrane interactions in this system is limited as the incorporation of integral and lipid-anchored proteins into GUVs remains challenging. Here, we present a simple generic method to incorporate proteins into GUVs. The basic principle is to break proteo-liposomes with an osmotic shock. They subsequently reseal into larger vesicles which, if necessary, can endure the same to obtain even larger proteo-GUVs. This process does not require specific lipids or reagents, works under physiological conditions with high concentrations of protein, the proteins remains functional after incorporation. The resulting proteo-GUVs can be micromanipulated. Moreover, our protocol is valid for a wide range of protein substrates. We have successfully reconstituted three structurally different proteins, two trans-membrane proteins (TolC and the neuronal t-SNARE), and one lipid-anchored peripheral protein (GABARAP-Like 1 (GL1)). In each case, we verified that the protein remains active after incorporation and in its correctly folded state. We also measured their mobility by performing diffusion measurements via fluorescence recovery after photobleaching (FRAP) experiments on micromanipulated single GUVs. The diffusion coefficients are in agreement with previous data.

Indexed as

Osmotic PressureCell MembraneDiffusionMembrane ProteinsModels, MolecularProtein MultimerizationProtein Structure, QuaternaryUnilamellar LiposomesMembrane ProteinsUnilamellar Liposomes

Identifiers

PMID26038815
PMCPMC4950989

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Registered trials

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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.