Evidence map›Paper›PMID 34210966›Full record

ArticleNature communications2021

Xanthomonas effector XopR hijacks host actin cytoskeleton via complex coacervation.

He Sun, Xinlu Zhu, Chuanxi Li, Zhiming Ma, Xiao Han, Yuanyuan Luo, Liang Yang, Jing Yu, Yansong Miao

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. 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
11.7field-weighted citation impact, top 1% 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, 74 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Resistance gene againstFrontiers in plant science · 2026
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. The Type III Effector XopLInternational journal of molecular sciences · 2024
    Article
  17. Review
  18. Article
  19. Functional Analysis of Type III Effectors inPathogens (Basel, Switzerland) · 2024
    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 1 institution in 1 country.

He SunSchool of Biological Sciences, Nanyang Technological University, Singapore, Singapore.
Xinlu ZhuSchool of Biological Sciences, Nanyang Technological University, Singapore, Singapore.
Chuanxi LiSchool of Materials Science and Engineering, Nanyang Technological University, Singapore, Singapore.
Zhiming MaSchool of Biological Sciences, Nanyang Technological University, Singapore, Singapore.
Xiao HanSchool of Biological Sciences, Nanyang Technological University, Singapore, Singapore.
Yuanyuan LuoSchool of Biological Sciences, Nanyang Technological University, Singapore, Singapore.
Liang YangSchool of Biological Sciences, Nanyang Technological University, Singapore, Singapore.ORCID 0000-0002-2362-0128
Jing YuSchool of Materials Science and Engineering, Nanyang Technological University, Singapore, Singapore.ORCID 0000-0002-4288-951X
Yansong MiaoSchool of Biological Sciences, Nanyang Technological University, Singapore, Singapore. yansongm@ntu.edu.sg.ORCID 0000-0003-1551-7873
Nanyang Technological University · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The intrinsically disordered region (IDR) is a preserved signature of phytobacterial type III effectors (T3Es). The T3E IDR is thought to mediate unfolding during translocation into the host cell and to avoid host defense by sequence diversification. Here, we demonstrate a mechanism of host subversion via the T3E IDR. We report that the Xanthomonas campestris T3E XopR undergoes liquid-liquid phase separation (LLPS) via multivalent IDR-mediated interactions that hijack the Arabidopsis actin cytoskeleton. XopR is gradually translocated into host cells during infection and forms a macromolecular complex with actin-binding proteins at the cell cortex. By tuning the physical-chemical properties of XopR-complex coacervates, XopR progressively manipulates multiple steps of actin assembly, including formin-mediated nucleation, crosslinking of F-actin, and actin depolymerization, which occurs through competition for actin-depolymerizing factor and depends on constituent stoichiometry. Our findings unravel a sophisticated strategy in which bacterial T3E subverts the host actin cytoskeleton via protein complex coacervation.

Indexed as

Actin CytoskeletonAgrobacteriumArabidopsisBacterial ProteinsIntrinsically Disordered ProteinsKineticsNicotianaPlants, Genetically ModifiedSequence AnalysisXanthomonasXanthomonas campestrisBacterial ProteinsIntrinsically Disordered Proteins

Identifiers

PMID34210966
PMCPMC8249405
OpenAlexW3174129339

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.