Evidence map›Paper›PMID 37902009›Full record

ArticleEMBO reports2023

Tetraspanner-based nanodomains modulate BAR domain-induced membrane curvature.

Daniel Haase, Christiane Rasch, Ulrike Keller, Yaroslav Tsytsyura, Nataliya Glyvuk, Annegret Elting, Julia Wittmar, Annette Janning, Martin Kahms, Noah Wedlich and 4 more

Open access · hybridAbstract read
In one paragraph

Article in EMBO reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.8field-weighted citation impact, top 27% 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

4 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Sur7 mediates a novel pathway for PIMolecular biology of the cell · 2024
    Article
  3. Article
  4. 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

14 authors at 2 institutions in 1 country.

Daniel HaaseInstitute of Cell Dynamics and Imaging, and Cells-in-Motion Interfaculty Center (CiMIC), University of Münster, Münster, Germany.ORCID 0000-0003-0973-1830
Christiane RaschInstitute for Medical Physics and Biophysics, and Cells-in-Motion Interfaculty Center (CiMIC), Münster, Germany.
Ulrike KellerInstitute for Medical Physics and Biophysics, and Cells-in-Motion Interfaculty Center (CiMIC), Münster, Germany.
Yaroslav TsytsyuraInstitute for Medical Physics and Biophysics, and Cells-in-Motion Interfaculty Center (CiMIC), Münster, Germany.ORCID 0009-0002-4332-0453
Nataliya GlyvukInstitute for Medical Physics and Biophysics, and Cells-in-Motion Interfaculty Center (CiMIC), Münster, Germany.ORCID 0009-0003-2603-134X
Annegret EltingInstitute of Cell Dynamics and Imaging, and Cells-in-Motion Interfaculty Center (CiMIC), University of Münster, Münster, Germany.
Julia WittmarInstitute of Cell Dynamics and Imaging, and Cells-in-Motion Interfaculty Center (CiMIC), University of Münster, Münster, Germany.ORCID 0000-0002-4063-3334
Annette JanningInstitute of Cell Dynamics and Imaging, and Cells-in-Motion Interfaculty Center (CiMIC), University of Münster, Münster, Germany.
Martin KahmsInstitute for Medical Physics and Biophysics, and Cells-in-Motion Interfaculty Center (CiMIC), Münster, Germany.
Noah WedlichInstitute of Cell Dynamics and Imaging, and Cells-in-Motion Interfaculty Center (CiMIC), University of Münster, Münster, Germany.
Christian SchuberthInstitute of Cell Dynamics and Imaging, and Cells-in-Motion Interfaculty Center (CiMIC), University of Münster, Münster, Germany.
Andreas HeuerInstitute for Physical Chemistry, Münster, Germany.
Jürgen KlingaufInstitute for Medical Physics and Biophysics, and Cells-in-Motion Interfaculty Center (CiMIC), Münster, Germany.
Roland Wedlich-SöldnerInstitute of Cell Dynamics and Imaging, and Cells-in-Motion Interfaculty Center (CiMIC), University of Münster, Münster, Germany.ORCID 0000-0002-1364-7589
University of Münster · DECenter for NanoScience · DE

Funding

Deutsche Forschungsgemeinschaft (DFG) SFB1348Deutsche Forschungsgemeinschaft (DFG) SFB1557Deutsche Forschungsgemeinschaft (DFG) SFB944
6 · The paper itself

Abstract

The topography of biological membranes is critical for formation of protein and lipid microdomains. One prominent example in the yeast plasma membrane (PM) are BAR domain-induced PM furrows. Here we report a novel function for the Sur7 family of tetraspanner proteins in the regulation of local PM topography. Combining TIRF imaging, STED nanoscopy, freeze-fracture EM and membrane simulations we find that Sur7 tetraspanners form multimeric strands at the edges of PM furrows, where they modulate forces exerted by BAR domain proteins at the furrow base. Loss of Sur7 tetraspanners or Sur7 displacement due to altered PIP2 homeostasis leads to increased PM invagination and a distinct form of membrane tubulation. Physiological defects associated with PM tubulation are rescued by synthetic anchoring of Sur7 to furrows. Our findings suggest a key role for tetraspanner proteins in sculpting local membrane domains. The maintenance of stable PM furrows depends on a balance between negative curvature at the base which is generated by BAR domains and positive curvature at the furrows' edges which is stabilized by strands of Sur7 tetraspanners.

Indexed as

ProteinsCell MembraneProteinsBAR domain proteinsmembrane curvatureplasma membranetetraspannersyeast

Identifiers

PMID37902009
PMCPMC10702824
OpenAlexW4388014044

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.