Evidence map›Paper›PMID 25664724›Full record

ArticleNature structural & molecular biology2015

Yersinia effector YopO uses actin as bait to phosphorylate proteins that regulate actin polymerization.

Wei Lin Lee, Jonathan M Grimes, Robert C Robinson

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

31 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Review
  3. Selective Inhibition ofPharmaceutics · 2025
    Article
  4. VopX, a novelmBio · 2025
    Article
  5. Modeling of Cu(II)-based protein spin labels using rotamer libraries.Physical chemistry chemical physics : PCCP · 2024
    Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. ArfGAP1 restrictsEMBO reports · 2018
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 2 countries.

Wei Lin Lee1] Institute of Molecular and Cell Biology, Agency for Science, Technology and Research (A*STAR), Singapore. [2] Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, UK.ORCID 0000000310487556
Jonathan M Grimes1] Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, UK. [2] Diamond Light Source, Oxfordshire, UK.
Robert C Robinson1] Institute of Molecular and Cell Biology, Agency for Science, Technology and Research (A*STAR), Singapore. [2] Department of Biochemistry, National University of Singapore, Singapore.
Agency for Science, Technology and Research · SGCentre for Human Genetics · GB

Funding

Wellcome Trust 090207/Z/09/ZWellcome Trust 090532Wellcome Trust 090532/Z/09/Z
6 · The paper itself

Abstract

Pathogenic Yersinia species evade host immune systems through the injection of Yersinia outer proteins (Yops) into phagocytic cells. One Yop, YopO, also known as YpkA, induces actin-filament disruption, impairing phagocytosis. Here we describe the X-ray structure of Yersinia enterocolitica YopO in complex with actin, which reveals that YopO binds to an actin monomer in a manner that blocks polymerization yet allows the bound actin to interact with host actin-regulating proteins. SILAC-MS and biochemical analyses confirm that actin-polymerization regulators such as VASP, EVL, WASP, gelsolin and the formin diaphanous 1 are directly sequestered and phosphorylated by YopO through formation of ternary complexes with actin. This leads to a model in which YopO at the membrane sequesters actin from polymerization while using the bound actin as bait to recruit, phosphorylate and misregulate host actin-regulating proteins to disrupt phagocytosis.

Indexed as

Models, MolecularActinsBacterial Outer Membrane ProteinsBacterial ProteinsBinding SitesCrystallography, X-RayPhagocytosisPhosphorylationPolymerizationProtein Serine-Threonine KinasesProtein Structure, TertiaryYersinia enterocoliticaActinsBacterial Outer Membrane ProteinsBacterial ProteinsProtein Serine-Threonine KinasesYopO protein, Yersinia enterocolitica

Identifiers

PMID25664724
PMCPMC4745138
OpenAlexW2081531926

What OpenQuestion holds

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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.