Evidence map›Paper›PMID 33216759›Full record

ArticlePLoS biology2020

Structure of the Lifeact-F-actin complex.

Alexander Belyy, Felipe Merino, Oleg Sitsel, Stefan Raunser

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

50 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Cryo-EM structure revealed a novel F-actin binding motif in abioRxiv : the preprint server for biology · 2025
    Article
  11. Article
  12. Article
  13. Structure of the F-tractin-F-actin complex.The Journal of cell biology · 2025
    Article
  14. Review
  15. Article
  16. Editorial: Cell structure and dynamics in the nematodeFrontiers in cell and developmental biology · 2025
    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

4 authors at 1 institution in 1 country.

Alexander BelyyDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany.ORCID 0000-0003-3106-6574
Felipe MerinoDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany.ORCID 0000-0003-4166-8747
Oleg SitselDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany.ORCID 0000-0002-4496-7489
Stefan RaunserDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany.ORCID 0000-0001-9373-3016
Max Planck Institute of Molecular Physiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lifeact is a short actin-binding peptide that is used to visualize filamentous actin (F-actin) structures in live eukaryotic cells using fluorescence microscopy. However, this popular probe has been shown to alter cellular morphology by affecting the structure of the cytoskeleton. The molecular basis for such artefacts is poorly understood. Here, we determined the high-resolution structure of the Lifeact-F-actin complex using electron cryo-microscopy (cryo-EM). The structure reveals that Lifeact interacts with a hydrophobic binding pocket on F-actin and stretches over 2 adjacent actin subunits, stabilizing the DNase I-binding loop (D-loop) of actin in the closed conformation. Interestingly, the hydrophobic binding site is also used by actin-binding proteins, such as cofilin and myosin and actin-binding toxins, such as the hypervariable region of TccC3 (TccC3HVR) from Photorhabdus luminescens and ExoY from Pseudomonas aeruginosa. In vitro binding assays and activity measurements demonstrate that Lifeact indeed competes with these proteins, providing an explanation for the altering effects of Lifeact on cell morphology in vivo. Finally, we demonstrate that the affinity of Lifeact to F-actin can be increased by introducing mutations into the peptide, laying the foundation for designing improved actin probes for live cell imaging.

Indexed as

ActinsAnimalsBacterial ToxinsBinding, CompetitiveBinding SitesCofilin 1Cryoelectron MicroscopyFluorescent DyesHEK293 CellsHumansHydrophobic and Hydrophilic InteractionsIn Vitro TechniquesMicrofilament ProteinsMicroscopy, ConfocalModels, MolecularMyosinsABP140 protein, S cerevisiaeActinsBacterial ToxinsCFL1 protein, humanCofilin 1Fluorescent DyesMicrofilament ProteinsMyosinsPeptide FragmentsRecombinant Fusion ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID33216759
PMCPMC7717565
OpenAlexW3098164025

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.