Evidence map›Paper›PMID 29362354›Full record

ArticleNature communications2018

Epsin and Sla2 form assemblies through phospholipid interfaces.

Maria M Garcia-Alai, Johannes Heidemann, Michal Skruzny, Anna Gieras, Haydyn D T Mertens, Dmitri I Svergun, Marko Kaksonen, Charlotte Uetrecht, Rob Meijers

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

32 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
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  6. Review
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  8. Epsin1-mediated exosomal sorting of Dll4 modulates the tubular-macrophage crosstalk in diabetic nephropathy.Molecular therapy : the journal of the American Society of Gene Therapy · 2023
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  11. Biophysical Characterization of Membrane Proteins.Methods in molecular biology (Clifton, N.J.) · 2023
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  12. Opening opportunities for KCommunications biology · 2022
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  13. Article
  14. Article
  15. Article
  16. Article
  17. Value of models for membrane budding.Current opinion in cell biology · 2021
    Review
  18. Article
  19. Article
  20. 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

9 authors at 6 institutions in 2 countries.

Maria M Garcia-AlaiEuropean Molecular Biology Laboratory (EMBL), Hamburg Outstation, Notkestrasse 85, 22607, Hamburg, Germany.
Johannes HeidemannHeinrich Pette Institute, Leibniz Institute for Experimental Virology, Martinistrasse 52, 20251, Hamburg, Germany.
Michal SkruznyLOEWE Center for Synthetic Microbiology (SYNMIKRO), Max Planck Institute for Terrestrial Microbiology, 35043, Marburg, Germany.
Anna GierasEuropean Molecular Biology Laboratory (EMBL), Hamburg Outstation, Notkestrasse 85, 22607, Hamburg, Germany.
Haydyn D T MertensEuropean Molecular Biology Laboratory (EMBL), Hamburg Outstation, Notkestrasse 85, 22607, Hamburg, Germany.
Dmitri I SvergunEuropean Molecular Biology Laboratory (EMBL), Hamburg Outstation, Notkestrasse 85, 22607, Hamburg, Germany.
Marko KaksonenDepartment of Biochemistry and NCCR Chemical Biology, University of Geneva, Quai Ernest-Ansermet 30, 1211, Geneva 4, Switzerland.
Charlotte UetrechtHeinrich Pette Institute, Leibniz Institute for Experimental Virology, Martinistrasse 52, 20251, Hamburg, Germany. charlotte.uetrecht@xfel.eu.ORCID http://orcid.org/0000-0002-1991-7922
Rob MeijersEuropean Molecular Biology Laboratory (EMBL), Hamburg Outstation, Notkestrasse 85, 22607, Hamburg, Germany. r.meijers@embl-hamburg.de.ORCID http://orcid.org/0000-0003-2872-6279
European Molecular Biology Laboratory · DELeibniz Institute of Virology (LIV) · DEEuropean Molecular Biology Laboratory · DELoewe Center for Synthetic Microbiology · DEUniversität Hamburg · DEUniversity of Geneva · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In clathrin-mediated endocytosis, adapter proteins assemble together with clathrin through interactions with specific lipids on the plasma membrane. However, the precise mechanism of adapter protein assembly at the cell membrane is still unknown. Here, we show that the membrane-proximal domains ENTH of epsin and ANTH of Sla2 form complexes through phosphatidylinositol 4,5-bisphosphate (PIP2) lipid interfaces. Native mass spectrometry reveals how ENTH and ANTH domains form assemblies by sharing PIP2 molecules. Furthermore, crystal structures of epsin Ent2 ENTH domain from S. cerevisiae in complex with PIP2 and Sla2 ANTH domain from C. thermophilum illustrate how allosteric phospholipid binding occurs. A comparison with human ENTH and ANTH domains reveal only the human ENTH domain can form a stable hexameric core in presence of PIP2, which could explain functional differences between fungal and human epsins. We propose a general phospholipid-driven multifaceted assembly mechanism tolerating different adapter protein compositions to induce endocytosis.

Indexed as

Protein DomainsAdaptor Proteins, Vesicular TransportAmino Acid SequenceBinding SitesCell MembraneChaetomiumCrystallography, X-RayEndocytosisFungal ProteinsHumansModels, MolecularPhosphatidylinositol 4,5-DiphosphateProtein BindingProtein MultimerizationSaccharomyces cerevisiaeSequence Homology, Amino AcidAdaptor Proteins, Vesicular TransportepsinFungal ProteinsPhosphatidylinositol 4,5-Diphosphate

Identifiers

PMID29362354
PMCPMC5780493
OpenAlexW2793872756

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.