Evidence map›Paper›PMID 22679020›Full record

ArticleThe Journal of biological chemistry2012

Structural basis for membrane binding specificity of the Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin-2 determined by Arl1 GTPase.

Kensuke Nakamura, Zhiqiu Man, Yong Xie, Ayako Hanai, Hisayoshi Makyio, Masato Kawasaki, Ryuichi Kato, Hye-Won Shin, Kazuhisa Nakayama, Soichi Wakatsuki

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

20 citing papers in PubMed, 40 citations in OpenAlex.

  1. Lysosomal homeostasis at the crossroads of neurodegeneration.The Journal of clinical investigation · 2026
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  5. A mechanical-thermodynamic model for understanding endocytosis of COVID-19 virus SARS-CoV-2.Proceedings of the Institution of Mechanical Engineers. Part C. Journal of mechanical engineering science · 2022
    Article
  6. Article
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  8. Article
  9. Deciphering the BAR code of membrane modulators.Cellular and molecular life sciences : CMLS · 2017
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Arf6 exchange factor EFA6 and endophilin directly interact at the plasma membrane to control clathrin-mediated endocytosis.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  15. Article
  16. Article
  17. Saving the neck from scission.Communicative & integrative biology · 2013
    Article
  18. Article
  19. Article
  20. Membrane curvature and its generation by BAR proteins.Trends in biochemical sciences · 2012
    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

10 authors at 3 institutions in 1 country.

Kensuke NakamuraStructural Biology Research Center, Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization, KEK, Tsukuba, Ibaraki 305-0801, Japan.
Zhiqiu Man
Yong Xie
Ayako Hanai
Hisayoshi Makyio
Masato Kawasaki
Ryuichi Kato
Hye-Won Shin
Kazuhisa Nakayama
Soichi Wakatsuki
High Energy Accelerator Research Organization · JPKyoto University · JPThe Graduate University for Advanced Studies, SOKENDAI · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Membrane-sculpting BAR (Bin/Amphiphysin/Rvs) domains form a crescent-shaped homodimer that can sense and induce membrane curvature through its positively charged concave face. We have recently shown that Arfaptin-2, which was originally identified as a binding partner for the Arf and Rac1 GTPases, binds to Arl1 through its BAR domain and is recruited onto Golgi membranes. There, Arfaptin-2 induces membrane tubules. Here, we report the crystal structure of the Arfaptin-2 BAR homodimer in complex with two Arl1 molecules bound symmetrically to each side, leaving the concave face open for membrane association. The overall structure of the Arl1·Arfaptin-2 BAR complex closely resembles that of the PX-BAR domain of sorting nexin 9, suggesting similar mechanisms underlying BAR domain targeting to specific organellar membranes. The Arl1·Arfaptin-2 BAR structure suggests that one of the two Arl1 molecules competes with Rac1, which binds to the concave face of the Arfaptin-2 BAR homodimer and may hinder its membrane association.

Indexed as

Protein MultimerizationAdaptor Proteins, Signal TransducingADP-Ribosylation FactorsCrystallography, X-RayGolgi ApparatusHumansIntracellular MembranesMembrane ProteinsProtein BindingProtein Structure, QuaternaryProtein Structure, Tertiaryrac1 GTP-Binding ProteinStructure-Activity RelationshipAdaptor Proteins, Signal TransducingADP-ribosylation factor related proteinsADP-Ribosylation FactorsARFIP2 protein, humanMembrane Proteinsrac1 GTP-Binding ProteinRAC1 protein, human

Identifiers

PMID22679020
PMCPMC3408144
OpenAlexW2139240786

What OpenQuestion holds

Textmetadata
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.