Evidence map›Paper›PMID 29099277›Full record

ArticleAutophagy2017

The intracellular microbial sensor NLRP4 directs Rho-actin signaling to facilitate Group A Streptococcus-containing autophagosome-like vacuole formation.

Takashi Nozawa, Chihiro Aikawa, Atsuko Minowa-Nozawa, Ichiro Nakagawa

Open access · bronzeAbstract read
In one paragraph

Article in Autophagy, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.5field-weighted citation impact, top 31% 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

13 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. Autophagy and Bacterial infections.Autophagy reports · 2025
    Review
  3. Article
  4. Interplay between group AMicrobiology and molecular biology reviews : MMBR · 2024
    Review
  5. Review
  6. Effects ofInfection and immunity · 2023
    Article
  7. The NLR gene family: from discovery to present day.Nature reviews. Immunology · 2023
    Review
  8. Review
  9. Mechanisms of TLR4-Mediated Autophagy and Nitroxidative Stress.Frontiers in cellular and infection microbiology · 2021
    Review
  10. Taurine AlleviatesFrontiers in immunology · 2021
    Article
  11. Review
  12. TBC1D9 regulates TBK1 activation through CaNature communications · 2020
    Article
  13. Review
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

4 authors at 1 institution in 1 country.

Takashi Nozawaa Department of Microbiology, Graduate School of Medicine , Kyoto University , Kyoto , Japan.
Chihiro Aikawaa Department of Microbiology, Graduate School of Medicine , Kyoto University , Kyoto , Japan.
Atsuko Minowa-Nozawaa Department of Microbiology, Graduate School of Medicine , Kyoto University , Kyoto , Japan.
Ichiro Nakagawaa Department of Microbiology, Graduate School of Medicine , Kyoto University , Kyoto , Japan.
Kyoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Xenophagy, also known as antibacterial autophagy, functions as a crucial defense system that can utilize intracellular pattern recognition sensors, such as NLRP4, to recognize and selectively eliminate bacterial pathogens. However, little is known about how NLRP4 regulates xenophagy. Here, we report that NLRP4 binds ARHGDIA (Rho GDP dissociation inhibitor α) to regulate Rho GTPase signaling and facilitate actin-mediated xenophagy. Specifically, NLRP4 is recruited to Group A Streptococcus (GAS) and colocalizes with GAS-containing autophagosome-like vacuoles (GcAVs), where it regulates ARHGDIA-Rho GTPase recruitment to promote autophagosome formation. The interaction between NLRP4, ARHGDIA, and Rho GTPases is regulated by ARHGDIA Tyr156 phosphorylation, which acts as a gate to induce Rho-mediated xenophagy. Moreover, ARHGDIA and Rho GTPase are involved in actin-mediated ATG9A recruitment to phagophores, facilitating elongation to form autophagosomes. Collectively, these findings demonstrate that NLRP4 functions as a Rho receptor complex to direct actin dynamics regulating xenophagy.

Indexed as

Adaptor Proteins, Signal TransducingAutophagosomesAutophagyAutophagy-Related ProteinsHeLa CellsHumansMembrane ProteinsPhosphorylationProtein TransportRepressor Proteinsrho GTP-Binding Proteinsrho Guanine Nucleotide Dissociation Inhibitor alphaStreptococcal InfectionsStreptococcus pyogenesVacuolesVesicular Transport ProteinsAdaptor Proteins, Signal TransducingARHGDIA protein, humanATG9A protein, humanAutophagy-Related ProteinsMembrane ProteinsNLRP4 protein, humanRepressor Proteinsrho GTP-Binding Proteinsrho Guanine Nucleotide Dissociation Inhibitor alphaVesicular Transport ProteinsARHGDIAautophagyGroup A StreptococcusNLRP4xenophagy

Identifiers

PMID29099277
PMCPMC5788493
OpenAlexW2765829666

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.