Evidence map›Paper›PMID 21980283›Full record

ArticlePLoS pathogens2011

Quantitative in vivo analyses reveal calcium-dependent phosphorylation sites and identifies a novel component of the Toxoplasma invasion motor complex.

Thomas Nebl, Judith Helena Prieto, Eugene Kapp, Brian J Smith, Melanie J Williams, John R Yates, Alan F Cowman, Christopher J Tonkin

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
6.5field-weighted citation impact, top 2% 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

55 citing papers in PubMed, 94 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Motility-dependent processes inbioRxiv : the preprint server for biology · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Dominique Soldati-Favre: BringingFrontiers in cellular and infection microbiology · 2022
    Article
  10. Identification ofFrontiers in cellular and infection microbiology · 2022
    Article
  11. Frontiers in cellular and infection microbiology · 2022
    Article
  12. Article
  13. Article
  14. Genetic Indicators for Calcium Signaling Studies in Toxoplasma gondii.Methods in molecular biology (Clifton, N.J.) · 2020
    Article
  15. Article
  16. Article
  17. Article
  18. Calcium signaling and the lytic cycle of the Apicomplexan parasite Toxoplasma gondii.Biochimica et biophysica acta. Molecular cell research · 2018
    Review
  19. Review
  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

8 authors at 3 institutions in 2 countries.

Thomas NeblThe Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia.
Judith Helena Prieto
Eugene Kapp
Brian J Smith
Melanie J Williams
John R Yates
Alan F Cowman
Christopher J Tonkin
Walter and Eliza Hall Institute of Medical Research · AUScripps Research Institute · USUniversity of Melbourne · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Apicomplexan parasites depend on the invasion of host cells for survival and proliferation. Calcium-dependent signaling pathways appear to be essential for micronemal release and gliding motility, yet the target of activated kinases remains largely unknown. We have characterized calcium-dependent phosphorylation events during Toxoplasma host cell invasion. Stimulation of live tachyzoites with Ca²⁺-mobilizing drugs leads to phosphorylation of numerous parasite proteins, as shown by differential 2-DE display of ³²[P]-labeled protein extracts. Multi-dimensional Protein Identification Technology (MudPIT) identified ∼546 phosphorylation sites on over 300 Toxoplasma proteins, including 10 sites on the actomyosin invasion motor. Using a Stable Isotope of Amino Acids in Culture (SILAC)-based quantitative LC-MS/MS analyses we monitored changes in the abundance and phosphorylation of the invasion motor complex and defined Ca²⁺-dependent phosphorylation patterns on three of its components--GAP45, MLC1 and MyoA. Furthermore, calcium-dependent phosphorylation of six residues across GAP45, MLC1 and MyoA is correlated with invasion motor activity. By analyzing proteins that appear to associate more strongly with the invasion motor upon calcium stimulation we have also identified a novel 15-kDa Calmodulin-like protein that likely represents the MyoA Essential Light Chain of the Toxoplasma invasion motor. This suggests that invasion motor activity could be regulated not only by phosphorylation but also by the direct binding of calcium ions to this new component.

Indexed as

CalciumHumansPhosphorylationProtozoan ProteinsToxoplasmaToxoplasmosisCalciumProtozoan Proteins

Identifiers

PMID21980283
PMCPMC3182922
OpenAlexW1996338896

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.