Evidence map›Paper›PMID 34001871›Full record

ArticleNature communications2021

Structure of the endocytic adaptor complex reveals the basis for efficient membrane anchoring during clathrin-mediated endocytosis.

Javier Lizarrondo, David P Klebl, Stephan Niebling, Marc Abella, Martin A Schroer, Haydyn D T Mertens, Katharina Veith, Roland Thuenauer, Dmitri I Svergun, Michal Skruzny and 3 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

9 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. VapA/Scs2 sustains polarized growth inMicrobial cell (Graz, Austria) · 2026
    Article
  3. Article
  4. Article
  5. Biophysical Characterization of Membrane Proteins.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. To the Surface and Back: Exo- and Endocytic Pathways inFrontiers in cell and developmental biology · 2021
    Review
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

13 authors at 5 institutions in 3 countries.

Javier Lizarrondo *European Molecular Biology Laboratory, Hamburg Outstation, Hamburg, Germany.
David P Klebl *School of Biomedical Sciences, Faculty of Biological Sciences and Astbury Centre for Structural and Molecular Biology, University of Leeds, Leeds, UK.ORCID 0000-0002-3581-8334
Stephan NieblingEuropean Molecular Biology Laboratory, Hamburg Outstation, Hamburg, Germany.
Marc AbellaDepartment of Systems and Synthetic Microbiology, Max Planck Institute for Terrestrial Microbiology and LOEWE Center for Synthetic Microbiology (SYNMIKRO), Marburg, Germany.
Martin A SchroerEuropean Molecular Biology Laboratory, Hamburg Outstation, Hamburg, Germany.ORCID 0000-0002-0747-3965
Haydyn D T MertensEuropean Molecular Biology Laboratory, Hamburg Outstation, Hamburg, Germany.ORCID 0000-0002-5664-744X
Katharina VeithEuropean Molecular Biology Laboratory, Hamburg Outstation, Hamburg, Germany.
Roland ThuenauerTechnology Platform Microscopy and Image Analysis, Heinrich Pette Institute, Leibniz Institute for Experimental Virology, Hamburg, Germany.
Dmitri I SvergunEuropean Molecular Biology Laboratory, Hamburg Outstation, Hamburg, Germany.ORCID 0000-0003-0830-5696
Michal SkruznyDepartment of Systems and Synthetic Microbiology, Max Planck Institute for Terrestrial Microbiology and LOEWE Center for Synthetic Microbiology (SYNMIKRO), Marburg, Germany.ORCID 0000-0003-4286-7684
Frank SobottSchool of Molecular and Cellular Biology, Faculty of Biological Sciences and Astbury Centre for Structural and Molecular Biology, University of Leeds, Leeds, UK.ORCID 0000-0001-9029-1865
Stephen P MuenchSchool of Biomedical Sciences, Faculty of Biological Sciences and Astbury Centre for Structural and Molecular Biology, University of Leeds, Leeds, UK.ORCID 0000-0001-6869-4414
Maria M Garcia-AlaiEuropean Molecular Biology Laboratory, Hamburg Outstation, Hamburg, Germany. garcia@embl-hamburg.de.ORCID 0000-0002-5200-7816
European Molecular Biology Laboratory · DEUniversity of Leeds · GBLoewe Center for Synthetic Microbiology · DEEuropean Molecular Biology Laboratory · DELeibniz Institute of Virology (LIV) · DE

Funding

Wellcome TrustWellcome Trust 108466/Z/15/ZWellcome Trust 208385/Z/17/Z
6 · The paper itself

Abstract

During clathrin-mediated endocytosis, a complex and dynamic network of protein-membrane interactions cooperate to achieve membrane invagination. Throughout this process in yeast, endocytic coat adaptors, Sla2 and Ent1, must remain attached to the plasma membrane to transmit force from the actin cytoskeleton required for successful membrane invagination. Here, we present a cryo-EM structure of a 16-mer complex of the ANTH and ENTH membrane-binding domains from Sla2 and Ent1 bound to PIP

Indexed as

Adaptor Proteins, Vesicular TransportBinding SitesCell MembraneClathrinCryoelectron MicroscopyCytoskeletal ProteinsEndocytosisModels, MolecularProtein MultimerizationProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsAdaptor Proteins, Vesicular TransportClathrinCytoskeletal ProteinsENT1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSLA2 protein, S cerevisiaeVesicular Transport Proteins

Identifiers

PMID34001871
PMCPMC8129110
OpenAlexW3162178495

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.