Evidence map›Paper›PMID 28923919›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Multiple interactions between an Arf/GEF complex and charged lipids determine activation kinetics on the membrane.

Deepti Karandur, Agata Nawrotek, John Kuriyan, Jacqueline Cherfils

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

29 citing papers in PubMed, 48 citations in OpenAlex.

  1. The cytokinesis regulator RacGAP1 is a Rac1-specific GAP on membranes.Protein science : a publication of the Protein Society · 2026
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  11. Molecular Dynamics Simulation of Lipid-Modified Signaling Proteins.Methods in molecular biology (Clifton, N.J.) · 2021
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  18. A network of phosphatidylinositol 4,5-bisphosphate binding sites regulates gating of the CaProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 4 institutions in 2 countries.

Deepti KarandurDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720.
Agata NawrotekLaboratoire de Biologie et Pharmacologie Appliquée, CNRS, Cachan 94235, France.
John KuriyanDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720; kuriyan@berkeley.edu jacqueline.cherfils@ens-paris-saclay.fr.
Jacqueline CherfilsLaboratoire de Biologie et Pharmacologie Appliquée, CNRS, Cachan 94235, France; kuriyan@berkeley.edu jacqueline.cherfils@ens-paris-saclay.fr.
École Normale Supérieure Paris-Saclay · FRHoward Hughes Medical Institute · USLaboratoire de Biologie et Pharmacologie Appliquée · FRUniversity of California, Berkeley · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Lipidated small GTPases and their regulators need to bind to membranes to propagate actions in the cell, but an integrated understanding of how the lipid bilayer exerts its effect has remained elusive. Here we focused on ADP ribosylation factor (Arf) GTPases, which orchestrate a variety of regulatory functions in lipid and membrane trafficking, and their activation by the guanine-nucleotide exchange factor (GEF) Brag2, which controls integrin endocytosis and cell adhesion and is impaired in cancer and developmental diseases. Biochemical and structural data are available that showed the exceptional efficiency of Arf activation by Brag2 on membranes. We determined the high-resolution crystal structure of unbound Brag2 containing the GEF (Sec7) and membrane-binding (pleckstrin homology) domains, revealing that it has a constitutively active conformation. We used this structure to analyze the interaction of uncomplexed Brag2 and of the myristoylated Arf1/Brag2 complex with a phosphatidylinositol bisphosphate (PIP

Indexed as

ADP-Ribosylation FactorsComputer SimulationCrystallizationDiphosphonatesGuanine Nucleotide Exchange FactorsLipid BilayersModels, ChemicalModels, MolecularProtein BindingProtein ConformationADP-Ribosylation FactorsDiphosphonatesGuanine Nucleotide Exchange FactorsLipid Bilayerscrystallographyguanine-nucleotide exchange factorlipidmolecular dynamicssmall GTPase

Identifiers

PMID28923919
PMCPMC5664517
OpenAlexW2755820127

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.