Evidence map›Paper›PMID 27385343›Full record

ArticleMolecular biology of the cell2016

Eps15 membrane-binding and -bending activity acts redundantly with Fcho1 during clathrin-mediated endocytosis.

Lei Wang, Adam Johnson, Michael Hanna, Anjon Audhya

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

17 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Adaptation and evolution of the sea anemoneEcology and evolution · 2022
    Article
  6. Article
  7. The TPLATE complex mediates membrane bending during plant clathrin-mediated endocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Membrane Heterogeneity Controls Cellular Endocytic Trafficking.Frontiers in cell and developmental biology · 2020
    Review
  13. Article
  14. Topography design in model membranes: Where biology meets physics.Experimental biology and medicine (Maywood, N.J.) · 2019
    Review
  15. Article
  16. Article
  17. 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

4 authors at 1 institution in 1 country.

Lei WangDepartment of Biomolecular Chemistry, University of Wisconsin-Madison School of Medicine and Public Health, Madison, WI 53706.
Adam JohnsonDepartment of Biomolecular Chemistry, University of Wisconsin-Madison School of Medicine and Public Health, Madison, WI 53706.
Michael HannaDepartment of Biomolecular Chemistry, University of Wisconsin-Madison School of Medicine and Public Health, Madison, WI 53706.
Anjon AudhyaDepartment of Biomolecular Chemistry, University of Wisconsin-Madison School of Medicine and Public Health, Madison, WI 53706 audhya@wisc.edu.
University of Wisconsin–Madison · US

Funding

Training Program In Molecular AND Cellular PharmacologyT32GM008688 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI AUDHYA, ANJON · 1998 to 2020
$6.0M
Molecular Mechanisms that Regulate Lysosomal Protein TransportR01GM088151 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI AUDHYA, ANJON · 2010 to 2019
$3.0M
NIGMS NIH HHS R01 GM088151NIGMS NIH HHS T32 GM008688
6 · The paper itself

Abstract

Clathrin coat assembly on membranes requires cytosolic adaptors and accessory proteins, which bridge triskeleons with the lipid bilayer and stabilize lattice architecture throughout the process of vesicle formation. In Caenorhabditis elegans, the prototypical AP-2 adaptor complex, which is activated by the accessory factor Fcho1 at the plasma membrane, is dispensable during embryogenesis, enabling us to define alternative mechanisms that facilitate clathrin-mediated endocytosis. Here we uncover a synthetic genetic interaction between C. elegans Fcho1 (FCHO-1) and Eps15 (EHS-1), suggesting that they function in a parallel and potentially redundant manner. Consistent with this idea, we find that the FCHO-1 EFC/F-BAR domain and the EHS-1 EH domains exhibit highly similar membrane-binding and -bending characteristics in vitro. Furthermore, we demonstrate a critical role for EHS-1 when FCHO-1 membrane-binding and -bending activity is specifically eliminated in vivo. Taken together, our data highlight Eps15 as an important membrane-remodeling factor, which acts in a partially redundant manner with Fcho proteins during the earliest stages of clathrin-mediated endocytosis.

Indexed as

Adaptor Protein Complex 2Adaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCell MembraneClathrinClathrin-Coated VesiclesCoated Pits, Cell-MembraneEndocytosisHeLa CellsHumansIntracellular Signaling Peptides and ProteinsMembrane ProteinsMembranesAdaptor Protein Complex 2Adaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportCaenorhabditis elegans ProteinsClathrinEhs-1 protein, C elegansIntracellular Signaling Peptides and ProteinsMembrane ProteinsPhosphoproteins

Identifiers

PMID27385343
PMCPMC5007088
OpenAlexW2462152936

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.