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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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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-000E-F0B3-8 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-000E-F0B4-6
Genre: Journal Article

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© 2012 Federation of European Biochemical Societies. Published by Elsevier B.V.
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 Creators:
Vowinckel, Jakob1, Author              
Stahlberg, Silke1, Author              
Paulmann, Nils1, Author              
Bluemlein, Katharina2, Author              
Grohmann, Maik1, Author              
Ralser, Markus2, Author              
Walther, Diego J.1, Author              
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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Free keywords: 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
 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, 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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Language(s): eng - English
 Dates: 2012-09-262012-11-02
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.febslet.2012.09.027
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Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 586 (21) Sequence Number: - Start / End Page: 3819 - 3824 Identifier: ISSN: 0014-5793
CoNE: /journals/resource/954925399501