Evidence map›Paper›PMID 26686473›Full record

ArticleScientific reports2015

Caspase-11 and caspase-1 differentially modulate actin polymerization via RhoA and Slingshot proteins to promote bacterial clearance.

Kyle Caution, Mikhail A Gavrilin, Mia Tazi, Apurva Kanneganti, Daniel Layman, Sheshadri Hoque, Kathrin Krause, Amal O Amer

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

32 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Regulation, Activation and Function of Caspase-11 during Health and Disease.International journal of molecular sciences · 2021
    Review
  10. Article
  11. An overview of the non-canonical inflammasome.Molecular aspects of medicine · 2020
    Review
  12. Review
  13. Article
  14. Article
  15. Involvement of the Actin Machinery in Programmed Cell Death.Frontiers in cell and developmental biology · 2020
    Review
  16. Article
  17. Article
  18. Article
  19. Methylomic Changes of Autophagy-Related Genes byFrontiers in cell and developmental biology · 2019
    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

8 authors at 4 institutions in 1 country.

Kyle CautionDepartment of Microbial Infection and Immunity, Center for Microbial Interface Biology, Columbus OH 43210.
Mikhail A GavrilinDorothy M. Davis Heart and Lung Research Institute, and The Ohio State University, Columbus OH 43210.
Mia TaziDepartment of Microbial Infection and Immunity, Center for Microbial Interface Biology, Columbus OH 43210.
Apurva KannegantiDepartment of Microbial Infection and Immunity, Center for Microbial Interface Biology, Columbus OH 43210.
Daniel LaymanDepartment of Microbial Infection and Immunity, Center for Microbial Interface Biology, Columbus OH 43210.
Sheshadri HoqueDepartment of Microbial Infection and Immunity, Center for Microbial Interface Biology, Columbus OH 43210.
Kathrin KrauseDepartment of Microbial Infection and Immunity, Center for Microbial Interface Biology, Columbus OH 43210.
Amal O AmerDepartment of Microbial Infection and Immunity, Center for Microbial Interface Biology, Columbus OH 43210.
Microbial ID (United States) · USInterface (United States) · USThe Ohio State University · USLung Institute · US

Funding

Role of caspases in Legionella pneumophila pulmonary infectionR01HL094586 · NHLBI · OHIO STATE UNIVERSITY · PI AMER, AMAL O · 2009 to 2013
$1.9M
Human susceptibility to Legionella infectionR21AI113477 · NIAID · OHIO STATE UNIVERSITY · PI AMER, AMAL O · 2015 to 2016
$434k
NHLBI NIH HHS R01 HL094586NIAID NIH HHS R21 AI113477
6 · The paper itself

Abstract

Inflammasomes are multiprotein complexes that include members of the NOD-like receptor family and caspase-1. Caspase-1 is required for the fusion of the Legionella vacuole with lysosomes. Caspase-11, independently of the inflammasome, also promotes phagolysosomal fusion. However, it is unclear how these proteases alter intracellular trafficking. Here, we show that caspase-11 and caspase-1 function in opposing manners to phosphorylate and dephosphorylate cofilin, respectively upon infection with Legionella. Caspase-11 targets cofilin via the RhoA GTPase, whereas caspase-1 engages the Slingshot phosphatase. The absence of either caspase-11 or caspase-1 maintains actin in the polymerized or depolymerized form, respectively and averts the fusion of pathogen-containing vacuoles with lysosomes. Therefore, caspase-11 and caspase-1 converge on the actin machinery with opposing effects to promote vesicular trafficking.

Indexed as

ActinsAnimalsCaspase 1Cofilin 1HumansInflammasomesLegionella pneumophilaLegionnaires' DiseaseLysosomesMiceMice, KnockoutMultiprotein ComplexesPhosphoprotein PhosphatasesReceptors, Cell SurfacerhoA GTP-Binding ProteinVacuolesActinsCaspase 1Cofilin 1InflammasomesMultiprotein ComplexesPhosphoprotein PhosphatasesReceptors, Cell SurfacerhoA GTP-Binding ProteinSSH1 protein, mouseVesicular Transport Proteins

Identifiers

PMID26686473
PMCPMC4685268
OpenAlexW2411706432

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.