Evidence map›Paper›PMID 22922484›Full record

ArticleJournal of molecular biology2012

Membrane binding and self-association of the epsin N-terminal homology domain.

Chun-Liang Lai, Christine C Jao, Edward Lyman, Jennifer L Gallop, Brian J Peter, Harvey T McMahon, Ralf Langen, Gregory A Voth

Open access · hybridAbstract read
In one paragraph

Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

36 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Value of models for membrane budding.Current opinion in cell biology · 2021
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. The Cytosolic Phospholipase ABiomolecules · 2020
    Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Protein Amphipathic Helix Insertion: A Mechanism to Induce Membrane Fission.Frontiers in cell and developmental biology · 2019
    Review
  17. Biophysics of membrane curvature remodeling at molecular and mesoscopic lengthscales.Journal of physics. Condensed matter : an Institute of Physics journal · 2018
    Article
  18. Article
  19. Membrane remodeling by amyloidogenic and non-amyloidogenic proteins studied by EPR.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2017
    Review
  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

8 authors at 5 institutions in 2 countries.

Chun-Liang LaiDepartment of Chemistry, Institute of Biophysical Dynamics, James Franck Institute, and Computation Institute, University of Chicago, 5735S Ellis Avenue, Chicago, IL 60637, USA.
Christine C Jao
Edward Lyman
Jennifer L Gallop
Brian J Peter
Harvey T McMahon
Ralf Langen
Gregory A Voth
MRC Laboratory of Molecular Biology · GBUniversity of Southern California · USChicago Institute for Psychoanalysis · USUniversity of Chicago · USUniversity of Delaware · US

Funding

New Method for Biomembrane SimulationsR01GM063796 · NIGMS · UNIVERSITY OF UTAH · PI VOTH, GREGORY A. · 2001 to 2025
$6.3M
Structural Analysis of Protein-Membrane InteractionR01GM063915 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI LANGEN, RALF · 2001 to 2012
$2.8M
Training in Genetic, Molecular and Cellular BiologyT32GM067587 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI STALLCUP, MICHAEL R · 2003 to 2012
$1.8M
Medical Research Council MC_U105178795NIGMS NIH HHS GM063915NIGMS NIH HHS R01 GM063796NIGMS NIH HHS R01 GM063915NIGMS NIH HHS T32 GM067587Wellcome Trust 092096
6 · The paper itself

Abstract

Epsin possesses a conserved epsin N-terminal homology (ENTH) domain that acts as a phosphatidylinositol 4,5-bisphosphate-lipid-targeting and membrane-curvature-generating element. Upon binding phosphatidylinositol 4,5-bisphosphate, the N-terminal helix (H(0)) of the ENTH domain becomes structured and aids in the aggregation of ENTH domains, which results in extensive membrane remodeling. In this article, atomistic and coarse-grained (CG) molecular dynamics (MD) simulations are used to investigate the structure and the stability of ENTH domain aggregates on lipid bilayers. EPR experiments are also reported for systems composed of different ENTH-bound membrane morphologies, including membrane vesicles as well as preformed membrane tubules. The EPR data are used to help develop a molecular model of ENTH domain aggregates on preformed lipid tubules that are then studied by CG MD simulation. The combined computational and experimental approach suggests that ENTH domains exist predominantly as monomers on vesiculated structures, while ENTH domains self-associate into dimeric structures and even higher-order oligomers on the membrane tubes. The results emphasize that the arrangement of ENTH domain aggregates depends strongly on whether the local membrane curvature is isotropic or anisotropic. The molecular mechanism of ENTH-domain-induced membrane vesiculation and tubulation and the implications of the epsin's role in clathrin-mediated endocytosis resulting from the interplay between ENTH domain membrane binding and ENTH domain self-association are also discussed.

Indexed as

Protein Structure, TertiaryAdaptor Proteins, Vesicular TransportCell MembraneElectron Spin Resonance SpectroscopyModels, MolecularMolecular Dynamics SimulationProtein BindingAdaptor Proteins, Vesicular Transportepsin

Identifiers

PMID22922484
PMCPMC3682188
OpenAlexW2161354487

What OpenQuestion holds

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LicenceCC BY
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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.