Evidence map›Paper›PMID 22397711›Full record

ArticleBiochemistry2012

Toxoplasma gondii profilin acts primarily to sequester G-actin while formins efficiently nucleate actin filament formation in vitro.

Kristen M Skillman, Wassim Daher, Christopher I Ma, Dominique Soldati-Favre, L David Sibley

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

22 citing papers in PubMed, 47 citations in OpenAlex.

  1. Review
  2. Myosin F controls actin organization and dynamics inMolecular biology of the cell · 2024
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Dehydroepiandrosterone Effect onMicroorganisms · 2021
    Article
  8. Profilin choreographs actin and microtubules in cells and cancer.International review of cell and molecular biology · 2020
    Article
  9. Emerging Functions of Actins and Actin Binding Proteins in Trypanosomatids.Frontiers in cell and developmental biology · 2020
    Review
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Review
  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

5 authors at 2 institutions in 2 countries.

Kristen M SkillmanDepartment of Molecular Microbiology, Washington University School of Medicine, St. Louis, Missouri 63110, United States.
Wassim Daher
Christopher I Ma
Dominique Soldati-Favre
L David Sibley
Washington University in St. Louis · USUniversity of Geneva · CH

Funding

PROTEIN SECRETION &INTRACELLULAR SURVIVAL BY TOXOPLASMAR01AI034036 · NIAID · WASHINGTON UNIVERSITY · PI SIBLEY, L. DAVID · 1993 to 2019
$7.9M
Targeting the Actin Cytoskeleton in ParasitesR01AI073155 · NIAID · WASHINGTON UNIVERSITY · PI SIBLEY, L. DAVID · 2007 to 2011
$1.7M
NIAID NIH HHS AI073155NIAID NIH HHS R01 AI034036NIAID NIH HHS R01 AI073155
6 · The paper itself

Abstract

Apicomplexan parasites employ gliding motility that depends on the polymerization of parasite actin filaments for host cell entry. Despite this requirement, parasite actin remains almost entirely unpolymerized at steady state; formation of filaments required for motility relies on a small repertoire of actin-binding proteins. Previous studies have shown that apicomplexan formins and profilin exhibit canonical functions on heterologous actins from higher eukaryotes; however, their biochemical properties on parasite actins are unknown. We therefore analyzed the impact of T. gondii profilin (TgPRF) and FH1-FH2 domains of two formin isoforms in T. gondii (TgFRM1 and TgFRM2) on the polymerization of T. gondii actin (TgACTI). Our findings based on in vitro assays demonstrate that TgFRM1-FH1-FH2 and TgFRM2-FH1-FH2 dramatically enhanced TgACTI polymerization in the absence of profilin, making them the sole protein factors known to initiate polymerization of this normally unstable actin. In addition, T. gondii formin domains were shown to both initiate polymerization and induce bundling of TgACTI filaments; however, they did not rely on TgPRF for these activities. In contrast, TgPRF sequestered TgACTI monomers, thus inhibiting polymerization even in the presence of formins. Collectively, these findings provide insight into the unusual control mechanisms of actin dynamics within the parasite.

Indexed as

Actin CytoskeletonActinsNucleotidesProfilinsProtein MultimerizationProtein Structure, QuaternaryProtozoan ProteinsToxoplasmaActinsNucleotidesProfilinsProtozoan Proteins

Identifiers

PMID22397711
PMCPMC3319672
OpenAlexW1998757281

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.