Evidence map›Paper›PMID 25216944›Full record

ArticleEMBO reports2014

Direct interaction of actin filaments with F-BAR protein pacsin2.

Julius Kostan, Ulrich Salzer, Albina Orlova, Imre Törö, Vesna Hodnik, Yosuke Senju, Juan Zou, Claudia Schreiner, Julia Steiner, Jari Meriläinen and 9 more

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.0field-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

38 citing papers in PubMed, 57 citations in OpenAlex.

  1. Trial
  2. Article
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  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. PACSIN proteins in vivo: Roles in development and physiology.Acta physiologica (Oxford, England) · 2022
    Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
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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

19 authors at 8 institutions in 7 countries.

Julius KostanDepartment of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Vienna, Austria.
Ulrich SalzerDepartment of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Vienna, Austria Department of Medical Biochemistry, Medical University of Vienna, Vienna, Austria.
Albina OrlovaDepartment of Biochemistry and Molecular Genetics, University of Virginia Medical Center, Charlottesville, VA, USA.
Imre TöröDepartment of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Vienna, Austria.
Vesna HodnikDepartment of Biology, Biotechnical Faculty, University of Ljubljana, Ljubljana, Slovenia.
Yosuke SenjuProgram in Cell and Molecular Biology, Institute of Biotechnology, University of Helsinki, Helsinki, Finland.
Juan ZouWellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh, UK.
Claudia SchreinerDepartment of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Vienna, Austria.
Julia SteinerDepartment of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Vienna, Austria.
Jari MeriläinenDepartment of Pathology, Haartman Institute, University of Helsinki, Helsinki, Finland.
Marko NikkiDepartment of Pathology, Haartman Institute, University of Helsinki, Helsinki, Finland.
Ismo VirtanenInstitute of Biomedicine/Anatomy, University of Helsinki, Helsinki, Finland.
Oliviero CarugoDepartment of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Vienna, Austria Department of Chemistry, University of Pavia, Pavia, Italy.
Juri RappsilberDepartment of Pathology, Haartman Institute, University of Helsinki, Helsinki, Finland Department of Biotechnology, Technological University of Berlin, Berlin, Germany.
Pekka LappalainenProgram in Cell and Molecular Biology, Institute of Biotechnology, University of Helsinki, Helsinki, Finland.
Veli-Pekka LehtoDepartment of Pathology, Haartman Institute, University of Helsinki, Helsinki, Finland.
Gregor AnderluhDepartment of Biology, Biotechnical Faculty, University of Ljubljana, Ljubljana, Slovenia National Institute of Chemistry, Ljubljana, Slovenia EN-FIST Centre of Excellence, Ljubljana, Slovena.
Edward H EgelmanDepartment of Biochemistry and Molecular Genetics, University of Virginia Medical Center, Charlottesville, VA, USA.
Kristina Djinović-CarugoDepartment of Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, Vienna, Austria Department of Biochemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, Ljubljana, Slovenia kristina.djinovic@univie.ac.at.
University of Helsinki · FIUniversity of Vienna · ATMax Perutz Labs · ATUniversity of Virginia Medical Center · USEN-FIST Centre of Excellence (Slovenia) · SITechnische Universität Berlin · DEUniversity of Ljubljana · SIWellcome Centre for Cell Biology · GB

Funding

Structural Studies of ActinR01GM081303 · NIGMS · UNIVERSITY OF VIRGINIA · PI EGELMAN, EDWARD H. · 2007 to 2016
$3.6M
Austrian Science Fund FWF I 1593Austrian Science Fund FWF I 525NIGMS NIH HHS GM081303NIGMS NIH HHS R01 GM081303Wellcome Trust 084229Wellcome Trust 091020Wellcome Trust 092076Wellcome Trust 103139Wellcome Trust 103139/Z/13/Z
6 · The paper itself

Abstract

Two mechanisms have emerged as major regulators of membrane shape: BAR domain-containing proteins, which induce invaginations and protrusions, and nuclear promoting factors, which cause generation of branched actin filaments that exert mechanical forces on membranes. While a large body of information exists on interactions of BAR proteins with membranes and regulatory proteins of the cytoskeleton, little is known about connections between these two processes. Here, we show that the F-BAR domain protein pacsin2 is able to associate with actin filaments using the same concave surface employed to bind to membranes, while some other tested N-BAR and F-BAR proteins (endophilin, CIP4 and FCHO2) do not associate with actin. This finding reveals a new level of complexity in membrane remodeling processes.

Indexed as

Actin CytoskeletonAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsBinding SitesCell MembraneChickensMicrotubule-Associated ProteinsMolecular Docking SimulationMolecular Sequence DataProtein BindingAdaptor Proteins, Signal TransducingMicrotubule-Associated Proteinscryo‐electron microscopyF‐actin bindingF‐BAR protein pacsin2membrane sculpting

Identifiers

PMID25216944
PMCPMC4253489
OpenAlexW2102586905

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.