Evidence map›Paper›PMID 26316537›Full record

ArticleThe Journal of biological chemistry2015

Host Cell-catalyzed S-Palmitoylation Mediates Golgi Targeting of the Legionella Ubiquitin Ligase GobX.

Yi-Han Lin, Alexandra G Doms, Eric Cheng, Byoungkwan Kim, Timothy R Evans, Matthias P Machner

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.8field-weighted citation impact, top 5% 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

40 citing papers in PubMed, 66 citations in OpenAlex.

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  11. Pathogens (Basel, Switzerland) · 2022
    Article
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  13. Open biology · 2022
    Review
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  16. Evolution and Adaptation ofBiomolecules · 2021
    Review
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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

6 authors at 2 institutions in 1 country.

Yi-Han LinFrom the Unit on Microbial Pathogenesis, Cell Biology and Metabolism Program, Eunice Kennedy Shriver NICHD, National Institutes of Health, Bethesda, Maryland 20892.
Alexandra G DomsFrom the Unit on Microbial Pathogenesis, Cell Biology and Metabolism Program, Eunice Kennedy Shriver NICHD, National Institutes of Health, Bethesda, Maryland 20892.
Eric ChengFrom the Unit on Microbial Pathogenesis, Cell Biology and Metabolism Program, Eunice Kennedy Shriver NICHD, National Institutes of Health, Bethesda, Maryland 20892.
Byoungkwan KimFrom the Unit on Microbial Pathogenesis, Cell Biology and Metabolism Program, Eunice Kennedy Shriver NICHD, National Institutes of Health, Bethesda, Maryland 20892.
Timothy R EvansFrom the Unit on Microbial Pathogenesis, Cell Biology and Metabolism Program, Eunice Kennedy Shriver NICHD, National Institutes of Health, Bethesda, Maryland 20892.
Matthias P MachnerFrom the Unit on Microbial Pathogenesis, Cell Biology and Metabolism Program, Eunice Kennedy Shriver NICHD, National Institutes of Health, Bethesda, Maryland 20892 machnerm@mail.nih.gov.
Eunice Kennedy Shriver National Institute of Child Health and Human Development · USNational Institutes of Health · US

Funding

Virulence strategies of the respiratory pathogen Legionella pneumophilaZIAHD008893 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI MACHNER, MATTHIAS · 2010 to 2025
$19.6M
Intramural NIH HHS ZIA HD008893PHS HHS 1ZIAHD008893-04
6 · The paper itself

Abstract

The facultative intracellular pathogen Legionella pneumophila, the causative agent of Legionnaires disease, infects and replicates within human alveolar macrophages. L. pneumophila delivers almost 300 effector proteins into the besieged host cell that alter signaling cascades and create conditions that favor intracellular bacterial survival. In order for the effectors to accomplish their intracellular mission, their activity needs to be specifically directed toward the correct host cell protein or target organelle. Here, we show that the L. pneumophila effector GobX possesses E3 ubiquitin ligase activity that is mediated by a central region homologous to mammalian U-box domains. Furthermore, we demonstrate that GobX exploits host cell S-palmitoylation to specifically localize to Golgi membranes. The hydrophobic palmitate moiety is covalently attached to a cysteine residue at position 175, which is part of an amphipathic α-helix within the C-terminal region of GobX. Site-directed mutagenesis of cysteine 175 or residues on the hydrophobic face of the amphipathic helix strongly attenuated palmitoylation and Golgi localization of GobX. Together, our study provides evidence that the L. pneumophila effector GobX exploits two post-translational modification pathways of host cells, ubiquitination and S-palmitoylation.

Indexed as

BiocatalysisGolgi ApparatusLegionella pneumophilaProtein TransportUbiquitin-Protein LigasesUbiquitin-Protein Ligasesbacterial pathogenesisclick chemistryDHHC proteinGolgiLegionella pneumophilaprotein palmitoylationtranslocated effectorubiquitylation (ubiquitination)

Identifiers

PMID26316537
PMCPMC4646218
OpenAlexW2235251534

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.