Evidence map›Paper›PMID 20418375›Full record

ArticleThe Journal of biological chemistry2010

Roles of amphipathic helices and the bin/amphiphysin/rvs (BAR) domain of endophilin in membrane curvature generation.

Christine C Jao, Balachandra G Hegde, Jennifer L Gallop, Prabhavati B Hegde, Harvey T McMahon, Ian S Haworth, Ralf Langen

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
–field-weighted citation impact
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

50 citing papers in PubMed.

  1. Article
  2. Review
  3. Proteomic analysis of the pyrenoid-traversing membranes ofbioRxiv : the preprint server for biology · 2025
    Article
  4. Article
  5. Review
  6. Molecular Dynamics Simulations of Curved Lipid Membranes.International journal of molecular sciences · 2022
    Review
  7. Article
  8. Article
  9. Article
  10. Protein Amphipathic Helix Insertion: A Mechanism to Induce Membrane Fission.Frontiers in cell and developmental biology · 2019
    Review
  11. Article
  12. Biophysics of membrane curvature remodeling at molecular and mesoscopic lengthscales.Journal of physics. Condensed matter : an Institute of Physics journal · 2018
    Article
  13. Membrane remodeling by amyloidogenic and non-amyloidogenic proteins studied by EPR.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2017
    Review
  14. Deciphering the BAR code of membrane modulators.Cellular and molecular life sciences : CMLS · 2017
    Review
  15. Article
  16. Article
  17. Review
  18. Review
  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

7 authors.

Christine C JaoZilkha Neurogenetic Institute, University of Southern California, Los Angeles, California 90033, USA.
Balachandra G Hegde
Jennifer L Gallop
Prabhavati B Hegde
Harvey T McMahon
Ian S Haworth
Ralf Langen

Funding

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 GM063915NIGMS NIH HHS T32 GM067587
6 · The paper itself

Abstract

Control of membrane curvature is required in many important cellular processes, including endocytosis and vesicular trafficking. Endophilin is a bin/amphiphysin/rvs (BAR) domain protein that induces vesicle formation by promotion of membrane curvature through membrane binding as a dimer. Using site-directed spin labeling and EPR spectroscopy, we show that the overall BAR domain structure of the rat endophilin A1 dimer determined crystallographically is maintained under predominantly vesiculating conditions. Spin-labeled side chains on the concave surface of the BAR domain do not penetrate into the acyl chain interior, indicating that the BAR domain interacts only peripherally with the surface of a curved bilayer. Using a combination of EPR data and computational refinement, we determined the structure of residues 63-86, a region that is disordered in the crystal structure of rat endophilin A1. Upon membrane binding, residues 63-75 in each subunit of the endophilin dimer form a slightly tilted, amphipathic alpha-helix that directly interacts with the membrane. In their predominant conformation, these helices are located orthogonal to the long axis of the BAR domain. In this conformation, the amphipathic helices are positioned to act as molecular wedges that induce membrane curvature along the concave surface of the BAR domain.

Indexed as

Protein Structure, SecondaryProtein Structure, TertiaryAcyltransferasesAmino Acid SequenceAnimalsCell MembraneComputer SimulationCrystallography, X-RayElectron Spin Resonance SpectroscopyLiposomesMembrane FluidityMicroscopy, ElectronModels, BiologicalModels, MolecularMolecular Dynamics SimulationMolecular Sequence Data2-acylglycerophosphate acyltransferaseAcyltransferasesLiposomesSpin Labels

Identifiers

PMID20418375
PMCPMC2888429

What OpenQuestion holds

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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.