Evidence map›Paper›PMID 21822290›Full record

ArticleNature2011

Modulation of Rab GTPase function by a protein phosphocholine transferase.

Shaeri Mukherjee, Xiaoyun Liu, Kohei Arasaki, Justin McDonough, Jorge E Galán, Craig R Roy

Open access · greenAbstract read
In one paragraph

Article in Nature, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 193 papers.

0numbers the graph read from it
0cells of the map it votes in
193citing papers in PubMed
17.5field-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

193 citing papers in PubMed, 323 citations in OpenAlex.

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  14. crANKing up the infection: ankyrin domains inInfection and immunity · 2024
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133 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Shaeri MukherjeeSection of Microbial Pathogenesis, Yale University School of Medicine, Boyer Center for Molecular Medicine, Yale University, New Haven, Connecticut, CT 06536, USA.
Xiaoyun Liu
Kohei Arasaki
Justin McDonough
Jorge E Galán
Craig R Roy
Yale University · US

Funding

Viral Pathogenesis and TherapeuticsU54AI057158 · NIAID · WADSWORTH CENTER · PI LEVY, DAVID E · 2003 to 2014
$100.8M
EVASION OF ANTIGEN PRESENTATION BY VACUOLAR PATHOGENSR01AI048770 · NIAID · YALE UNIVERSITY · PI ROY, CRAIG R. · 2001 to 2015
$5.8M
Genetic Analysis of Legionella Phagosome TraffickingR01AI041699 · NIAID · YALE UNIVERSITY · PI ROY, CRAIG R. · 2002 to 2011
$4.1M
Modulation of Host Cell Functions by Coxiella burnetiiR01AI064559 · NIAID · YALE UNIVERSITY · PI ROY, CRAIG R. · 2006 to 2010
$1.8M
A Systems Biology Approach for Investigating Coxiella burneti InfectionF32AI082927 · NIAID · YALE UNIVERSITY · PI MCDONOUGH, JUSTIN ANDREW · 2009 to 2010
$98k
NIAID NIH HHS F32 AI082927NIAID NIH HHS R01 AI041699NIAID NIH HHS R01 AI048770NIAID NIH HHS R01-AI048770NIAID NIH HHS R01 AI064559NIAID NIH HHS R01-AI064559NIAID NIH HHS U54 AI057158NIAID NIH HHS U54-AI057158
6 · The paper itself

Abstract

The intracellular pathogen Legionella pneumophila modulates the activity of host GTPases to direct the transport and assembly of the membrane-bound compartment in which it resides. In vitro studies have indicated that the Legionella protein DrrA post-translationally modifies the GTPase Rab1 by a process called AMPylation. Here we used mass spectrometry to investigate post-translational modifications to Rab1 that occur during infection of host cells by Legionella. Consistent with in vitro studies, DrrA-mediated AMPylation of a conserved tyrosine residue in the switch II region of Rab1 was detected during infection. In addition, a modification to an adjacent serine residue in Rab1 was discovered, which was independent of DrrA. The Legionella effector protein AnkX was required for this modification. Biochemical studies determined that AnkX directly mediates the covalent attachment of a phosphocholine moiety to Rab1. This phosphocholine transferase activity used CDP-choline as a substrate and required a conserved histidine residue located in the FIC domain of the AnkX protein. During infection, AnkX modified both Rab1 and Rab35, which explains how this protein modulates membrane transport through both the endocytic and exocytic pathways of the host cell. Thus, phosphocholination of Rab GTPases represents a mechanism by which bacterial FIC-domain-containing proteins can alter host-cell functions.

Indexed as

AnimalsBacterial ProteinsChlorocebus aethiopsCOS CellsDiacylglycerol CholinephosphotransferaseGuanine Nucleotide Exchange FactorsHEK293 CellsHost-Pathogen InteractionsHumansLegionella pneumophilaLegionnaires' DiseaseMass SpectrometryProtein Processing, Post-Translationalrab GTP-Binding ProteinsBacterial ProteinsDiacylglycerol CholinephosphotransferaseGuanine Nucleotide Exchange Factorsrab GTP-Binding ProteinsSidM protein, Legionella pneumophila

Identifiers

PMID21822290
PMCPMC3206611
OpenAlexW2011747741

What OpenQuestion holds

Textmetadata
LicenceTDM
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.