Evidence map›Paper›PMID 37948300›Full record

ArticleJournal of the American Chemical Society2023

Molecular Sensing and Manipulation of Protein Oligomerization in Membrane Nanotubes with Bolaamphiphilic Foldamers.

Kathrin Aftahy, Pedro Arrasate, Pavel V Bashkirov, Petr I Kuzmin, Victor Maurizot, Ivan Huc, Vadim A Frolov

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 40% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. Nanoscale dynamics of Dynamin 1 helices reveals squeeze-twist deformation mode critical for membrane fission.Proceedings of the National Academy of Sciences of the United States of America · 2024
    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

7 authors at 6 institutions in 4 countries.

Kathrin AftahyDepartment of Pharmacy, Ludwig-Maximilians-Universität München, Munich 81377, Germany.
Pedro ArrasateBiofisika Institute (CSIC, UPV/EHU), University of the Basque Country, Leioa 48940, Spain.
Pavel V BashkirovResearch Institute for Systems Biology and Medicine, Moscow 117246, Russia.
Petr I KuzminA.N. Frumkin Institute of Physical Chemistry and Electrochemistry, Moscow 119071, Russia.
Victor MaurizotUniv. Bordeaux, CNRS, Bordeaux Institut National Polytechnique, CBMN (UMR 5248), Pessac 33600, France.ORCID 0000-0001-6104-796X
Ivan HucDepartment of Pharmacy, Ludwig-Maximilians-Universität München, Munich 81377, Germany.ORCID 0000-0001-7036-9696
Vadim A FrolovBiofisika Institute (CSIC, UPV/EHU), University of the Basque Country, Leioa 48940, Spain.
Ludwig-Maximilians-Universität München · DECentre National de la Recherche Scientifique · FRFrumkin Institute of Physical Chemistry and Electrochemistry · RUIkerbasque · ESInSysBio (Russia) · RUUniversity of the Basque Country · ES

Funding

Functional nanoscopy of membrane deformations and fission by dynamin superfamily membersR01GM121725 · NIGMS · UNIVERSITY OF CALIF-LAWRNC LVRMR NAT LAB · PI FROLOV, VADIM A, NOY, ALEKSANDR · 2017 to 2021
$2.3M
NIGMS NIH HHS R01 GM121725
6 · The paper itself

Abstract

Adaptive and reversible self-assembly of supramolecular protein structures is a fundamental characteristic of dynamic living matter. However, the quantitative detection and assessment of the emergence of mesoscale protein complexes from small and dynamic oligomeric precursors remains highly challenging. Here, we present a novel approach utilizing a short membrane nanotube (sNT) pulled from a planar membrane reservoir as nanotemplates for molecular reconstruction, manipulation, and sensing of protein oligomerization and self-assembly at the mesoscale. The sNT reports changes in membrane shape and rigidity caused by membrane-bound proteins as variations of the ionic conductivity of the sNT lumen. To confine oligomerization to the sNT, we have designed and synthesized rigid oligoamide foldamer tapes (ROFTs). Charged ROFTs incorporate into the planar and sNT membranes, mediate protein binding to the membranes, and, driven by the luminal electric field, shuttle the bound proteins between the sNT and planar membranes. Using Annexin-V (AnV) as a prototype, we show that the sNT detects AnV oligomers shuttled into the nanotube by ROFTs. Accumulation of AnV on the sNT induces its self-assembly into a curved lattice, restricting the sNT geometry and inhibiting the material uptake from the reservoir during the sNT extension, leading to the sNT fission. By comparing the spontaneous and ROFT-mediated entry of AnV into the sNT, we reveal how intricate membrane curvature sensing by small AnV oligomers controls the lattice self-assembly. These results establish sNT-ROFT as a powerful tool for molecular reconstruction and functional analyses of protein oligomerization and self-assembly, with broad application to various membrane processes.

Indexed as

Membrane ProteinsNanotubesProtein BindingMembrane Proteins

Identifiers

PMID37948300
PMCPMC10682987
OpenAlexW4388563666

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.