Pluripotency and a secretion mechanism of Drosophila transglutaminase

研究成果: Contribution to journalReview article査読

3 被引用数 (Scopus)

抄録

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.

本文言語英語
ページ(範囲)165-176
ページ数12
ジャーナルJournal of biochemistry
163
3
DOI
出版ステータス出版済み - 3 1 2018

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

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