Evidence map›Paper›PMID 35589838›Full record

ArticleNature structural & molecular biology2022

Allosteric regulation controls actin-bundling properties of human plastins.

Christopher L Schwebach, Elena Kudryashova, Richa Agrawal, Weili Zheng, Edward H Egelman, Dmitri S Kudryashov

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
–field-weighted citation impact
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

18 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Actin isoform-specific interactions revealed byProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Effects of Bile on PathogenicBiomolecules · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Fascin structural plasticity mediates flexible actin bundle construction.bioRxiv : the preprint server for biology · 2024
    Article
  12. Stabilization of F-actin bybioRxiv : the preprint server for biology · 2023
    Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Structural mechanism for bidirectional actin cross-linking by T-plastin.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  18. International journal of molecular sciences · 2022
    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

6 authors.

Christopher L SchwebachDepartment of Chemistry and Biochemistry, Ohio State University, Columbus, OH, USA.ORCID 0000-0002-5595-8641
Elena KudryashovaDepartment of Chemistry and Biochemistry, Ohio State University, Columbus, OH, USA.ORCID 0000-0002-1646-1229
Richa AgrawalDepartment of Chemistry and Biochemistry, Ohio State University, Columbus, OH, USA.
Weili ZhengDepartment of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA, USA.
Edward H EgelmanDepartment of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA, USA.ORCID 0000-0003-4844-5212
Dmitri S KudryashovDepartment of Chemistry and Biochemistry, Ohio State University, Columbus, OH, USA. kudryashov.1@osu.edu.ORCID 0000-0003-1782-3305

Funding

Cryo-EM of Helical Protein and Nucleoprotein Polymers at Near Atomic ResolutionR35GM122510 · NIGMS · UNIVERSITY OF VIRGINIA · PI EDWARD H. EGELMAN · 2017 to 2026
$7.3M
Name Molecular mechanisms of bacterial toxins targeting actin cytoskeletonR01GM114666 · NIGMS · OHIO STATE UNIVERSITY · PI KUDRYASHOV, DMITRI · 2015 to 2025
$3.8M
NIGMS NIH HHS R01 GM114666NIGMS NIH HHS R35 GM122510
6 · The paper itself

Abstract

Plastins/fimbrins are conserved actin-bundling proteins contributing to motility, cytokinesis and other cellular processes by organizing strikingly different actin assemblies as in aligned bundles and branched networks. We propose that this ability of human plastins stems from an allosteric communication between their actin-binding domains (ABD1/2) engaged in a tight spatial association. Here we show that ABD2 can bind actin three orders of magnitude stronger than ABD1, unless the domains are involved in an equally strong inhibitory engagement. A mutation mimicking physiologically relevant phosphorylation at the ABD1-ABD2 interface greatly weakened their association, dramatically potentiating actin cross-linking. Cryo-EM reconstruction revealed the ABD1-actin interface and enabled modeling of the plastin bridge and domain separation in parallel bundles. We predict that a strong and tunable allosteric inhibition between the domains allows plastins to modulate the cross-linking strength, contributing to remodeling of actin assemblies of different morphologies defining the unique place of plastins in actin organization.

Indexed as

ActinsMicrofilament ProteinsActin CytoskeletonAllosteric RegulationHumansMembrane GlycoproteinsActinsMembrane GlycoproteinsMicrofilament Proteinsplastin

Identifiers

PMID35589838
PMCPMC9358775

What OpenQuestion holds

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Registered trials

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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.