Evidence map›Paper›PMID 22307087›Full record

ArticleThe EMBO journal2012

Reversible phosphocholination of Rab proteins by Legionella pneumophila effector proteins.

Philip R Goody, Katharina Heller, Lena K Oesterlin, Matthias P Müller, Aymelt Itzen, Roger S Goody

Abstract read
In one paragraph

Article in The EMBO journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
–field-weighted citation impact
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

62 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Pathogens (Basel, Switzerland) · 2022
    Article
  6. Glycosylating Effectors ofBiomolecules · 2022
    Review
  7. Review
  8. Article
  9. Article
  10. Proteolysis of Rab32 byiScience · 2021
    Article
  11. Review
  12. Interesting Biochemistries in the Structure and Function of Bacterial Effectors.Frontiers in cellular and infection microbiology · 2021
    Review
  13. Review
  14. Review
  15. Host Epigenetics in Intracellular Pathogen Infections.International journal of molecular sciences · 2020
    Review
  16. Science advances · 2020
    Article
  17. Conformational control of small GTPases by AMPylation.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  18. Phosphoinositides and the Fate ofFrontiers in immunology · 2020
    Review
  19. Review
  20. Study ofInfection and immunity · 2019
    Article

2 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

6 authors.

Philip R GoodyDepartment of Physical Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, Germany.
Katharina Heller
Lena K Oesterlin
Matthias P Müller
Aymelt Itzen
Roger S Goody

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Legionella pneumophila protein AnkX that is injected into infected cells by a Type IV secretion system transfers a phosphocholine group from CDP-choline to a serine in the Rab1 and Rab35 GTPase Switch II regions. We show here that the consequences of phosphocholination on the interaction of Rab1/Rab35 with various partner proteins are quite distinct. Activation of phosphocholinated Rabs by GTP/GDP exchange factors (GEFs) and binding to the GDP dissociation inhibitor (GDI) are strongly inhibited, whereas deactivation by GTPase activating proteins (GAPs) and interactions with Rab-effector proteins (such as LidA and MICAL-3) are only slightly inhibited. We show that the Legionella protein lpg0696 has the ability to remove the phosphocholine group from Rab1. We present a model in which the action of AnkX occurs as an alternative to GTP/GDP exchange, stabilizing phosphocholinated Rabs in membranes in the GDP form because of loss of GDI binding ability, preventing interactions with cellular GTPase effectors, which require the GTP-bound form. Generation of the GTP form of phosphocholinated Rab proteins cannot occur due to loss of interaction with cellular GEFs.

Indexed as

Bacterial ProteinsGTPase-Activating ProteinsGTP PhosphohydrolasesGuanine Nucleotide Exchange FactorsLegionella pneumophilaPhosphorylcholinerab GTP-Binding ProteinsBacterial ProteinsGTPase-Activating ProteinsGTP PhosphohydrolasesGuanine Nucleotide Exchange FactorsPhosphorylcholinerab GTP-Binding Proteins

Identifiers

PMID22307087
PMCPMC3321196

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.