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

Vowinckel, J., Stahlberg, S., Paulmann, N., Bluemlein, K., Grohmann, M., Ralser, M., et al. (2012). Histaminylation of glutamine residues is a novel posttranslational modification implicated in G-protein signaling. FEBS Letters, 586(21), 3819-3824. doi:10.1016/j.febslet.2012.09.027.

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© 2012 Federation of European Biochemical Societies. Published by Elsevier B.V.
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 Urheber:
Vowinckel, Jakob1, Autor           
Stahlberg, Silke1, Autor           
Paulmann, Nils1, Autor           
Bluemlein, Katharina2, Autor           
Grohmann, Maik1, Autor           
Ralser, Markus2, Autor           
Walther, Diego J.1, Autor           
Affiliations:
1Dept. of Human Molecular Genetics (Head: Hans-Hilger Ropers), Max Planck Institute for Molecular Genetics, Max Planck Society, Berlin, Germany, ou_1433549              
2Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society, Berlin, Germany, ou_1433550              

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Schlagwörter: Amino Acid Sequence Animals Catalytic Domain Cell Line, Tumor Escherichia coli/genetics GTP-Binding Protein alpha Subunits, Gi-Go/genetics/*metabolism GTP-Binding Protein alpha Subunits, Gq-G11/genetics/*metabolism GTP-Binding Proteins/genetics/*metabolism Gene Expression Glutamine/genetics/metabolism Histamine/genetics/*metabolism Mass Spectrometry Mastocytoma/enzymology/genetics Mice Molecular Sequence Data *Protein Processing, Post-Translational Proteome/genetics/metabolism Recombinant Fusion Proteins/genetics/metabolism Signal Transduction/genetics Transglutaminases/genetics/*metabolism cdc42 GTP-Binding Protein/genetics/*metabolism
 Zusammenfassung: 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, Galphao1 and Galphaq. 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 alphamonoaminylations, thus including histaminylation, serotonylation, dopaminylation and norepinephrinylation, hence emerge as a novel class of regulatory PTMs.

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Sprache(n): eng - English
 Datum: 2012-09-262012-11-02
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1016/j.febslet.2012.09.027
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Titel: FEBS Letters
  Andere : FEBS Lett.
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Amsterdam : Elsevier
Seiten: - Band / Heft: 586 (21) Artikelnummer: - Start- / Endseite: 3819 - 3824 Identifikator: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501