Evidence map›Paper›PMID 23184949›Full record

ArticleThe Journal of biological chemistry2013

Identification of a His-Asp-Cys catalytic triad essential for function of the Rho inactivation domain (RID) of Vibrio cholerae MARTX toxin.

Sebastian Ahrens, Brett Geissler, Karla J F Satchell

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

28 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Antagonistic effects of actin-specific toxins onbioRxiv : the preprint server for biology · 2024
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  4. Chemical Proteomics Reveals NMolecular & cellular proteomics : MCP · 2024
    Article
  5. Article
  6. International journal of molecular sciences · 2022
    Article
  7. TheScience signaling · 2020
    Article
  8. Article
  9. Review
  10. Article
  11. NNature microbiology · 2018
    Article
  12. Review
  13. EnteropathogenicCellular and molecular gastroenterology and hepatology · 2018
    Article
  14. Review
  15. Article
  16. Article
  17. Review
  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

3 authors at 1 institution in 1 country.

Sebastian AhrensDepartment of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60611, USA.
Brett Geissler
Karla J F Satchell
Northwestern University · US

Funding

Genetic and biochemical study ov V. cholerase RTX toxinR01AI051490 · NIAID · NORTHWESTERN UNIVERSITY AT CHICAGO · PI SATCHELL, KARLA J F · 2003 to 2012
$3.3M
NIAID NIH HHS R01 AI051490
6 · The paper itself

Abstract

Vibrio cholerae is the causative agent of the severe diarrheal disease cholera. For V. cholerae to colonize the intestinal epithelium, accessory toxins such as the multifunctional autoprocessing repeats-in-toxin (MARTX(Vc)) toxin are required. MARTX toxins are composite toxins comprised of arrayed effector domains that carry out distinct functions inside the host cell. Among the three effector domains of MARTX(Vc) is the Rho inactivation domain (RID(Vc)) known to cause cell rounding through inactivation of small RhoGTPases. Using alanine scanning mutagenesis in the activity subdomain of RID(Vc), four residues, His-2782, Leu-2851, Asp-2854, and Cys-3022, were identified as impacting RID(Vc) function in depolymerization of the actin cytoskeleton and inactivation of RhoA. Tyr-2807 and Tyr-3015 were identified as important potentially for forming the active structure for substrate contact but are not involved in catalysis or post translational modifications. Finally, V. cholerae strains modified to carry a catalytically inactive RID(Vc) show that the rate and efficiency of MARTX(Vc) actin cross-linking activity does not depend on a functional RID(Vc), demonstrating that these domains function independently in actin depolymerization. Overall, our results indicate a His-Asp-Cys catalytic triad is essential for function of the RID effector domain family shared by MARTX toxins produced by many Gram-negative bacteria.

Indexed as

ActinsAmino Acid SequenceBacterial ToxinsCatalytic DomainChromosomes, BacterialCircular DichroismHeLa CellsHumansMolecular Sequence DataMutagenesis, Site-DirectedOligopeptidesrho GTP-Binding ProteinsSequence Homology, Amino AcidVibrio choleraeActinsBacterial ToxinsOligopeptidesrho GTP-Binding ProteinsRtxA protein, Vibrio cholerae

Identifiers

PMID23184949
PMCPMC3543022
OpenAlexW2093735326

What OpenQuestion holds

Textmetadata
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.