Evidence map›Paper›PMID 25865245›Full record

ArticleStructure (London, England : 1993)2015

Tubulation by amphiphysin requires concentration-dependent switching from wedging to scaffolding.

J Mario Isas, Mark R Ambroso, Prabhavati B Hegde, Jennifer Langen, Ralf Langen

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Dynamics of membrane tubulation coupled with fission by a two-component module.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Generation of nanoscopic membrane curvature for membrane trafficking.Nature reviews. Molecular cell biology · 2023
    Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. The plasma membrane as a mechanochemical transducer.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2019
    Review
  17. Article
  18. Article
  19. Protein Amphipathic Helix Insertion: A Mechanism to Induce Membrane Fission.Frontiers in cell and developmental biology · 2019
    Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

J Mario IsasZilkha Neurogenetic Institute, University of Southern California, 1501 San Pablo Street, Los Angeles, CA 90033, USA.
Mark R AmbrosoZilkha Neurogenetic Institute, University of Southern California, 1501 San Pablo Street, Los Angeles, CA 90033, USA.
Prabhavati B HegdeZilkha Neurogenetic Institute, University of Southern California, 1501 San Pablo Street, Los Angeles, CA 90033, USA.
Jennifer LangenDepartment of Biological Sciences, University of Southern California, Los Angeles, CA 90089-2910, USA.
Ralf LangenZilkha Neurogenetic Institute, University of Southern California, 1501 San Pablo Street, Los Angeles, CA 90033, USA. Electronic address: langen@usc.edu.

Funding

Structural Analysis of Protein-Membrane InteractionR01GM063915 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI LANGEN, RALF · 2001 to 2012
$2.8M
NIGMS NIH HHS GM063915NIGMS NIH HHS R01 GM063915
6 · The paper itself

Abstract

BAR proteins are involved in a variety of membrane remodeling events but how they can mold membranes into different shapes remains poorly understood. Using electron paramagnetic resonance, we find that vesicle binding of the N-BAR protein amphiphysin is predominantly mediated by the shallow insertion of amphipathic N-terminal helices. In contrast, the interaction with tubes involves deeply inserted N-terminal helices together with the concave surface of the BAR domain, which acts as a scaffold. Combined with the observed concentration dependence of tubulation and BAR domain scaffolding, the data indicate that initial membrane deformations and vesicle binding are mediated by insertion of amphipathic helical wedges, while tubulation requires high protein densities at which oligomeric BAR domain scaffolds form. In addition, we identify a pocket of residues on the concave surface of the BAR domain that insert deeply into tube membrane. Interestingly, this pocket harbors a number of disease mutants in the homologous amphiphysin 2.

Indexed as

AnimalsBinding SitesCell MembraneCrystallography, X-RayDrosophilaDrosophila ProteinsLipid-Linked ProteinsModels, BiologicalModels, MolecularNerve Tissue ProteinsProtein BindingProtein Structure, SecondaryamphiphysinDrosophila ProteinsLipid-Linked ProteinsNerve Tissue Proteins

Identifiers

PMID25865245
PMCPMC4437528

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.