Evidence map›Paper›PMID 24120140›Full record

ArticleCell2013

The bacterial effector VopL organizes actin into filament-like structures.

Jacob A Zahm, Shae B Padrick, Zhucheng Chen, Chi W Pak, Ali A Yunus, Lisa Henry, Diana R Tomchick, Zhe Chen, Michael K Rosen

Abstract read
In one paragraph

Article in Cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

35 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Cryo-EM structure revealed a novel F-actin binding motif in abioRxiv : the preprint server for biology · 2025
    Article
  5. ADPact: A versatile sensor for ADP-F-actin.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Review
  7. Article
  8. Article
  9. Membrane-dependent actin polymerization mediated by thebioRxiv : the preprint server for biology · 2023
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Orchestrated actin nucleation by theThe Journal of biological chemistry · 2020
    Article
  15. Article
  16. Improved strategy for isoleucineJournal of biomolecular NMR · 2019
    Article
  17. Article
  18. Article
  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

9 authors at 3 institutions in 1 country.

Jacob A ZahmDepartment of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA; Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Shae B Padrick
Zhucheng Chen
Chi W Pak
Ali A Yunus
Lisa Henry
Diana R Tomchick
Zhe Chen
Michael K Rosen
Howard Hughes Medical Institute · USSouthwestern Medical Center · USThe University of Texas Southwestern Medical Center · US

Funding

STRUCTURAL STUDY OF RHO-GTPASE REGULATORS AND EFFECTORSR01GM056322 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI ROSEN, MICHAEL K · 1997 to 2019
$5.7M
Molecular Biophysics Predoctoral Training ProgramT32GM008297 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI CHOOK, YUH MIN · 1989 to 2018
$2.4M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM056322NIGMS NIH HHS R01-GM56322NIGMS NIH HHS T32 GM008297
6 · The paper itself

Abstract

VopL is an effector protein from Vibrio parahaemolyticus that nucleates actin filaments. VopL consists of a VopL C-terminal domain (VCD) and an array of three WASP homology 2 (WH2) motifs. Here, we report the crystal structure of the VCD dimer bound to actin. The VCD organizes three actin monomers in a spatial arrangement close to that found in the canonical actin filament. In this arrangement, WH2 motifs can be modeled into the binding site of each actin without steric clashes. The data suggest a mechanism of nucleation wherein VopL creates filament-like structures, organized by the VCD with monomers delivered by the WH2 array, that can template addition of new subunits. Similarities with Arp2/3 complex and formin proteins suggest that organization of monomers into filament-like structures is a general and central feature of actin nucleation.

Indexed as

Actin CytoskeletonActinsAnimalsBacterial ProteinsCrystallography, X-RayModels, MolecularProtein Structure, TertiaryRabbitsVibrio parahaemolyticusActinsBacterial Proteins

Identifiers

PMID24120140
PMCPMC4048032
OpenAlexW2027472513

What OpenQuestion holds

Textmetadata
LicenceTDM
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.