Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The Legionella pneumophila effector DenR hijacks the host NRas proto-oncoprotein to downregulate MAPK signaling

1 Apr 2024

Abstract excerpt

Small GTPases of the Ras subfamily are best known for their role as proto-oncoproteins, while their function during microbial infection has remained elusive. Here, we show that Legionella pneumophila hijacks the small GTPase NRas to the Legionella-containing vacuole (LCV) surface. A CRISPR interference screen identifies a single L. pneumophila effector, DenR (Lpg1909), required for this process. Recruitment is...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Autophagy in Disease and Therapy
Share to Legionella and Acanthamoeba research
Share to Neutrophil, Myeloperoxidase and Oxidative Mechanisms

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 38568811
DOI: 10.1016/j.celrep.2024.114033

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The Legionella pneumophila effector DenR hijacks the host NRas proto-oncoprotein to downregulate MAPK signalingPMID 38568811Read ↗

Cross-family small GTPase ubiquitination by the intracellular pathogen Legionella pneumophilaSemantic proximity Read ↗

A Burkholderia Type VI Effector Deamidates Rho GTPases to Activate the Pyrin Inflammasome and Trigger InflammationSemantic proximity Read ↗

The Legionella pneumophila effector protein DrrA is a Rab1 guanine nucleotide-exchange factor.Semantic proximity Read ↗

Phosphoribosyl ubiquitination of SNARE proteins regulate autophagy in Legionella infectionSemantic proximity Read ↗

Genetic identification of the RAS proteostatic machinery and its failure to regulate oncogenic variantsSemantic proximity Read ↗

ARHGEF26 enhances Salmonella invasion and inflammation in cells and mice.Semantic proximity Read ↗

Structural mechanism for guanylate-binding proteins (GBPs) targeting by the Shigella E3 ligase IpaH9.8Semantic proximity Read ↗

Autophagy‐linked plasma and lysosomal membrane protein PLAC8 is a key host factor for SARS‐CoV‐2 entry into human cellsSemantic proximity Read ↗

A CRISPR-Cas9 screen Reveals STEEP1 as a Key Host Dependency Factor for Epstein-Barr Virus Latent Membrane Protein 1 Trafficking and SignalingSemantic proximity Read ↗

Phosphoribosyl ubiquitination of SNARE proteins regulates autophagy during Legionella infectionSemantic proximity Read ↗

Klebsiella pneumoniae Reduces SUMOylation To Limit Host Defense ResponsesSemantic proximity Read ↗

Atypical Legionella GTPase effector hijacks host vesicular transport factor p115 to regulate host lipid dropletSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.