Evidence map›Paper›PMID 22158903›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Legionella pneumophila regulates the small GTPase Rab1 activity by reversible phosphorylcholination.

Yunhao Tan, Randy J Arnold, Zhao-Qing Luo

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 117 papers.

0numbers the graph read from it
0cells of the map it votes in
117citing papers in PubMed
9.6field-weighted citation impact, top 1% 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

117 citing papers in PubMed, 197 citations in OpenAlex.

  1. Article
  2. Molecular evolution and adaptations ofFrontiers in cellular and infection microbiology · 2026
    Review
  3. Systematic Discovery of Novel Phosphoinositide-Binding Effectors inbioRxiv : the preprint server for biology · 2025
    Article
  4. Article
  5. mLife · 2025
    Article
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57 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

Yunhao TanDepartment of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA.
Randy J Arnold
Zhao-Qing Luo
Purdue University West Lafayette · USIndiana University Bloomington · US

Funding

Modulation of host Apoptotic pathways by Legionella pneumophilaR01AI069344 · NIAID · PURDUE UNIVERSITY · PI LUO, ZHAO-QING · 2007 to 2011
$1.5M
Modulation of Host Vesicle Trafficking by Legionella pneumophilaK02AI085403 · NIAID · PURDUE UNIVERSITY · PI LUO, ZHAO-QING · 2010 to 2014
$556k
The Roles of Host Factors in the AMPylation Activity of a Bacterial EffectorR21AI092043 · NIAID · PURDUE UNIVERSITY · PI LUO, ZHAO-QING · 2011 to 2012
$413k
NIAID NIH HHS K02 AI085403NIAID NIH HHS K02AI085403NIAID NIH HHS R01 AI069344NIAID NIH HHS R01AI069344NIAID NIH HHS R21 AI092043NIAID NIH HHS R21AI092043
6 · The paper itself

Abstract

Effectors delivered into host cells by the Legionella pneumophila Dot/Icm type IV transporter are essential for the biogenesis of the specialized vacuole that permits its intracellular growth. The biochemical function of most of these effectors is unknown, making it difficult to assign their roles in the establishment of successful infection. We found that several yeast genes involved in membrane trafficking, including the small GTPase Ypt1, strongly suppress the cytotoxicity of Lpg0695(AnkX), a protein known to interfere severely with host vesicle trafficking when overexpressed. Mass spectrometry analysis of Rab1 purified from a yeast strain inducibly expressing AnkX revealed that this small GTPase is modified posttranslationally at Ser(76) by a phosphorylcholine moiety. Using cytidine diphosphate-choline as the donor for phosphorylcholine, AnkX catalyzes the transfer of phosphorylcholine to Rab1 in a filamentation-induced by cAMP(Fic) domain-dependent manner. Further, we found that the activity of AnkX is regulated by the Dot/Icm substrate Lpg0696(Lem3), which functions as a dephosphorylcholinase to reverse AnkX-mediated modification on Rab1. Phosphorylcholination interfered with Rab1 activity by making it less accessible to the bacterial GTPase activation protein LepB; this interference can be alleviated fully by Lem3. Our results reveal reversible phosphorylcholination as a mechanism for balanced modulation of host cellular processes by a bacterial pathogen.

Indexed as

Bacterial ProteinsCytidine Diphosphate CholineDNA PrimersGene Expression ProfilingGTP PhosphohydrolasesGuanine Nucleotide Exchange FactorsHost-Pathogen InteractionsImmunoblottingLegionella pneumophilaMass SpectrometryMembrane Transport ProteinsPhosphorylcholineProtein Processing, Post-Translationalrab1 GTP-Binding ProteinsSequence Analysis, DNAYeastsBacterial ProteinsCytidine Diphosphate CholineDNA PrimersGTP PhosphohydrolasesGuanine Nucleotide Exchange FactorsLepB protein, Legionella pneumophilaMembrane Transport ProteinsPhosphorylcholinerab1 GTP-Binding ProteinsSidM protein, Legionella pneumophila

Identifiers

PMID22158903
PMCPMC3248503
OpenAlexW2047410466

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.