Pluripotency and a secretion mechanism of Drosophila transglutaminase

Toshio Shibata, Shun Ichiro Kawabata

Research output: Contribution to journalReview articlepeer-review

8 Citations (Scopus)


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-iB-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.

Original languageEnglish
Pages (from-to)165-176
Number of pages12
JournalJournal of biochemistry
Issue number3
Publication statusPublished - Mar 1 2018

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology


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