Evidence map›Paper›PMID 23022564›Full record

ArticleFEBS letters2012

Histaminylation of glutamine residues is a novel posttranslational modification implicated in G-protein signaling.

Jakob Vowinckel, Silke Stahlberg, Nils Paulmann, Katharina Bluemlein, Maik Grohmann, Markus Ralser, Diego J Walther

Open access · hybridAbstract read
In one paragraph

Article in FEBS letters, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

19 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
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  6. Article
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  11. Review
  12. TGM2-mediated histone transglutamination is dictated by steric accessibility.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  13. Diamine oxidase knockout mice are not hypersensitive to orally or subcutaneously administered histamine.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2022
    Article
  14. Review
  15. Review
  16. Serotonylation: Serotonin Signaling and Epigenetics.Frontiers in molecular neuroscience · 2019
    Review
  17. Article
  18. Transglutaminase 2-mediated serotonylation in pulmonary hypertension.American journal of physiology. Lung cellular and molecular physiology · 2014
    Review
  19. Review
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

7 authors at 3 institutions in 2 countries.

Jakob VowinckelMax Planck Institute for Molecular Genetics, Berlin, Germany. jv330@cam.ac.uk
Silke Stahlberg
Nils Paulmann
Katharina Bluemlein
Maik Grohmann
Markus Ralser
Diego J Walther
Max Planck Institute for Molecular Genetics · DEUniversity of Cambridge · GBFreie Universität Berlin · DE

Funding

European Research Council 260809Wellcome TrustWellcome Trust RG 093735/Z/10/Z
6 · The paper itself

Abstract

Posttranslational modifications (PTM) have been shown to be essential for protein function and signaling. Here we report the identification of a novel modification, protein transfer of histamine, and provide evidence for its function in G protein signaling. Histamine, known as neurotransmitter and mediator of the inflammatory response, was found incorporated into mastocytoma proteins. Histaminylation was dependent on transglutaminase II. Mass spectrometry confirmed histamine modification of the small and heterotrimeric G proteins Cdc42, Gαo1 and Gαq. The modification was specific for glutamine residues in the catalytic core, and triggered their constitutive activation. TGM2-mediated histaminylation is thus a novel PTM that functions in G protein signaling. Protein αmonoaminylations, thus including histaminylation, serotonylation, dopaminylation and norepinephrinylation, hence emerge as a novel class of regulatory PTMs.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceAnimalsCatalytic Domaincdc42 GTP-Binding ProteinCell Line, TumorEscherichia coliGene ExpressionGlutamineGTP-Binding Protein alpha Subunits, Gi-GoGTP-Binding Protein alpha Subunits, Gq-G11GTP-Binding ProteinsHistamineMass SpectrometryMastocytomaMicecdc42 GTP-Binding ProteinGlutamineGTP-Binding Protein alpha Subunits, Gi-GoGTP-Binding Protein alpha Subunits, Gq-G11GTP-Binding ProteinsHistamineProtein Glutamine gamma Glutamyltransferase 2ProteomeRecombinant Fusion ProteinsTransglutaminases

Identifiers

PMID23022564
PMCPMC3743044
OpenAlexW2031266047

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.