Evidence map›Paper›PMID 23638681›Full record

ArticleTraffic (Copenhagen, Denmark)2013

Global analysis of apicomplexan protein S-acyl transferases reveals an enzyme essential for invasion.

Karine Frénal, Chwen L Tay, Christina Mueller, Ellen S Bushell, Yonggen Jia, Arnault Graindorge, Oliver Billker, Julian C Rayner, Dominique Soldati-Favre

Open access · hybridAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

44 citing papers in PubMed, 86 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. SPARK regulates AGC kinases central to thebioRxiv : the preprint server for biology · 2024
    Article
  6. Article
  7. Microorganisms · 2023
    Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Protein S-palmitoylation in cellular differentiation.Biochemical Society transactions · 2017
    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

9 authors at 2 institutions in 2 countries.

Karine FrénalDepartment of Microbiology and Molecular Medicine, CMU, University of Geneva, Rue Michel-Servet 1, CH-1211, Geneva 4, Switzerland.
Chwen L Tay
Christina Mueller
Ellen S Bushell
Yonggen Jia
Arnault Graindorge
Oliver Billker
Julian C Rayner
Dominique Soldati-Favre
University of Geneva · CHWellcome Sanger Institute · GB

Funding

Howard Hughes Medical InstituteMedical Research Council G0501670Medical Research Council G0501670)Wellcome TrustWellcome Trust WT098051
6 · The paper itself

Abstract

The advent of techniques to study palmitoylation on a whole proteome scale has revealed that it is an important reversible modification that plays a role in regulating multiple biological processes. Palmitoylation can control the affinity of a protein for lipid membranes, which allows it to impact protein trafficking, stability, folding, signalling and interactions. The publication of the palmitome of the schizont stage of Plasmodium falciparum implicated a role for palmitoylation in host cell invasion, protein export and organelle biogenesis. However, nothing is known so far about the repertoire of protein S-acyl transferases (PATs) that catalyse this modification in Apicomplexa. We undertook a comprehensive analysis of the repertoire of Asp-His-His-Cys cysteine-rich domain (DHHC-CRD) PAT family in Toxoplasma gondii and Plasmodium berghei by assessing their localization and essentiality. Unlike functional redundancies reported in other eukaryotes, some apicomplexan-specific DHHCs are essential for parasite growth, and several are targeted to organelles unique to this phylum. Of particular interest is DHHC7, which localizes to rhoptry organelles in all parasites tested, including the major human pathogen P. falciparum. TgDHHC7 interferes with the localization of the rhoptry palmitoylated protein TgARO and affects the apical positioning of the rhoptry organelles. This PAT has a major impact on T. gondii host cell invasion, but not on the parasite's ability to egress.

Indexed as

AcetyltransferasesAmino Acid MotifsCell Culture TechniquesGene DeletionGenome, ProtozoanHumansPhylogenyPlasmodium bergheiProtein Structure, TertiaryProtein TransportProtozoan ProteinsToxoplasmaAcetyltransferasesprotein acyltransferaseProtozoan ProteinsApicomplexaegressinvasionpalmitoyl acyl transferasepalmitoylationPlasmodium bergheiPlasmodium falciparumrhoptry organelleToxoplasma gondii

Identifiers

PMID23638681
PMCPMC3813974
OpenAlexW1550685405

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.