Evidence map›Paper›PMID 33513092›Full record

ArticleeLife2021

Nanoscopic anatomy of dynamic multi-protein complexes at membranes resolved by graphene-induced energy transfer.

Nadia Füllbrunn, Zehao Li, Lara Jorde, Christian P Richter, Rainer Kurre, Lars Langemeyer, Changyuan Yu, Carola Meyer, Jörg Enderlein, Christian Ungermann and 2 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

10 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Article
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  7. Article
  8. Structure of the Mon1-Ccz1 complex reveals molecular basis of membrane binding for Rab7 activation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Review
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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

12 authors at 3 institutions in 2 countries.

Nadia Füllbrunn *Department of Biology/Chemistry, University of Osnabrück, Osnabrück, Germany.
Zehao Li *Department of Biology/Chemistry, University of Osnabrück, Osnabrück, Germany.
Lara JordeDepartment of Physics, University of Osnabrück, Osnabrück, Germany.
Christian P RichterDepartment of Biology/Chemistry, University of Osnabrück, Osnabrück, Germany.
Rainer KurreDepartment of Biology/Chemistry, University of Osnabrück, Osnabrück, Germany.
Lars LangemeyerDepartment of Biology/Chemistry, University of Osnabrück, Osnabrück, Germany.ORCID 0000-0002-4309-0910
Changyuan YuCollege of Life Sciences, Beijing University of Chemical Technology, Beijing, China.
Carola MeyerCenter of Cellular Nanoanalytics (CellNanOs), University of Osnabrück, Osnabrück, Germany.ORCID 0000-0003-0851-2767
Jörg Enderlein3rd Institute of Physics - Biophysics, Georg August University, Göttingen, Germany.ORCID 0000-0001-5091-7157
Christian UngermannDepartment of Biology/Chemistry, University of Osnabrück, Osnabrück, Germany.ORCID 0000-0003-4331-8695
Jacob PiehlerDepartment of Biology/Chemistry, University of Osnabrück, Osnabrück, Germany.ORCID 0000-0002-2143-2270
Changjiang YouDepartment of Biology/Chemistry, University of Osnabrück, Osnabrück, Germany.ORCID 0000-0002-7839-6397
Osnabrück University · DEBeijing University of Chemical Technology · CNMultiscale Bioimaging

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Insights into the conformational organization and dynamics of proteins complexes at membranes is essential for our mechanistic understanding of numerous key biological processes. Here, we introduce graphene-induced energy transfer (GIET) to probe axial orientation of arrested macromolecules at lipid monolayers. Based on a calibrated distance-dependent efficiency within a dynamic range of 25 nm, we analyzed the conformational organization of proteins and complexes involved in tethering and fusion at the lysosome-like yeast vacuole. We observed that the membrane-anchored Rab7-like GTPase Ypt7 shows conformational reorganization upon interactions with effector proteins. Ensemble and time-resolved single-molecule GIET experiments revealed that the HOPS tethering complex, when recruited via Ypt7 to membranes, is dynamically alternating between a 'closed' and an 'open' conformation, with the latter possibly interacting with incoming vesicles. Our work highlights GIET as a unique spectroscopic ruler to reveal the axial orientation and dynamics of macromolecular complexes at biological membranes with sub-nanometer resolution.

Indexed as

Cell MembraneGraphiteMultiprotein ComplexesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsGraphiteMultiprotein ComplexesSaccharomyces cerevisiae Proteinsconformational dynamicsgraphene induced energy transferHOPS tethering complexmembrane proteinmolecular biophysicsprotein conformationS. cerevisiaestructural biology

Identifiers

PMID33513092
PMCPMC7847308
OpenAlexW3124480512

What OpenQuestion holds

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LicenceCC BY
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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.