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

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• 作者：Jakob Vowinckel^a ; ^b ; ^{jv330@cam.ac.uk} ; Silke Stahlberg^a ; ^c ; Nils Paulmann^a ; Katharina Bluemlein^b ; Maik Grohmann^a ; Markus Ralser^a ; ^b ; ¹ ; ^{mr559@cam.ac.uk} ; Diego J. Walther^a ; ¹ ; ^{dwalther@molgen.mpg.de}
• 关键词：HA ; histamine ; PTM ; posttranslational modification ; TGM ; transglutaminase ; SRM ; selective reaction monitoring ; CTA ; cysteamine
• 刊名：FEBS Letters
• 出版年：2012
• 出版时间：2 November, 2012
• 年：2012
• 卷：586
• 期：21
• 页码：3819-3824
• 全文大小：705 K

文摘

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, G¦Áo1 and G¦Áq. 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 ¦Ámonoaminylations, thus including histaminylation, serotonylation, dopaminylation and norepinephrinylation, hence emerge as a novel class of regulatory PTMs.

Structured summary of protein interactions

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