Pluripotency and a secretion mechanism of Drosophila transglutaminase

研究成果: ジャーナルへの寄稿評論記事

2 引用 (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.

元の言語英語
ページ(範囲)165-176
ページ数12
ジャーナルJournal of biochemistry
163
発行部数3
DOI
出版物ステータス出版済み - 3 1 2018

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Transglutaminases
Drosophila
Glutamine
Exosomes
Acylation
Immune Tolerance
Chitin
Hemolymph
Alternative Splicing
Polyamines
Pathogens
Coagulation
Morphogenesis
Endoplasmic Reticulum
Lysine
Amines
Bacteria
Carrier Proteins
Protein Isoforms
Proteins

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

これを引用

Pluripotency and a secretion mechanism of Drosophila transglutaminase. / Shibata, Toshio; Kawabata, Shun-Ichiro.

:: Journal of biochemistry, 巻 163, 番号 3, 01.03.2018, p. 165-176.

研究成果: ジャーナルへの寄稿評論記事

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