Pluripotency and a secretion mechanism of Drosophila transglutaminase

Transglutaminase (TG) catalyses the formation of an isopeptide bond between glutamine and lysine residues and amine incorporation into specific glutamine residues. TG is conserved in all metazoans and functions both intracellularly and extracellularly. Here we review the existing knowledge of Drosop...

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Bibliographic Details
Published in:Journal of biochemistry (Tokyo) 2018-03, Vol.163 (3), p.165-176
Main Authors: Shibata, Toshio, Kawabata, Shun-Ichiro
Format: Article
Language:English
Subjects:
Animals
Drosophila - enzymology
Drosophila - metabolism
Drosophila Proteins - metabolism
Endoplasmic Reticulum - metabolism
Golgi Apparatus - metabolism
Polyamines - metabolism
Transcription Factors - metabolism
Transglutaminases - immunology
Transglutaminases - metabolism
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Summary:Transglutaminase (TG) catalyses the formation of an isopeptide bond between glutamine and lysine residues and amine incorporation into specific glutamine residues. TG is conserved in all metazoans and functions both intracellularly and extracellularly. Here we review the existing knowledge of Drosophila TG with an emphasis on its pluripotency: Drosophila TG (i) plays a key role in cuticular morphogenesis, haemolymph coagulation, and entrapment against invading pathogens, (ii) suppresses the immune deficiency pathway to enable immune tolerance against commensal bacteria through the incorporation of polyamines into the nuclear factor-κB-like transcription factor Relish as well as through the protein-protein cross-linking of Relish, (iii) forms a physical matrix in the gut through cross-linking of chitin-binding proteins and (iv) is involved in the maintenance of homeostasis in microbiota in the gut. Moreover, we review the evidence that TG-A, one of alternative splicing-derived isoforms of Drosophila TG, is secreted through an endoplasmic reticulum/Golgi-independent pathway involving exosomes and fatty acylations.
ISSN:0021-924X
1756-2651
DOI:10.1093/jb/mvx059