| http://purl.uniprot.org/citations/28476891 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/28476891 | http://www.w3.org/2000/01/rdf-schema#comment | "Transglutaminases (TGs) play essential intracellular and extracellular roles by covalently cross-linking many proteins. Drosophila TG is encoded by one gene and has two alternative splicing-derived isoforms, TG-A and TG-B, which contain distinct N-terminal 46- and 38-amino acid sequences, respectively. The TGs identified to date do not have a typical endoplasmic reticulum (ER)-signal peptide, and the molecular mechanisms of their secretion under physiologic conditions are unclear. Immunocytochemistry revealed that TG-A localizes to multivesicular-like structures, whereas TG-B localizes to the cytosol. We also found that TG-A, but not TG-B, was modified concomitantly by N-myristoylation and S-palmitoylation, and N-myristoylation was a pre-requisite for S-palmitoylation. Moreover, TG-A, but not TG-B, was secreted in response to calcium signaling induced by Ca2+ ionophores and uracil, a pathogenic bacteria-derived substance. Brefeldin A and monensin, inhibitors of the ER/Golgi-mediated conventional pathway, did not suppress TG-A secretion, whereas inhibition of S-palmitoylation by 2-bromopalmitate blocked TG-A secretion. Ultracentrifugation, electron microscopy analyses, and treatments with inhibitors of multivesicular body formation revealed that TG-A was secreted via exosomes together with co-transfected mammalian CD63, an exosomal marker, and the secreted TG-A was taken up by other cells. The 8-residue N-terminal fragment of TG-A containing the fatty acylation sites was both necessary and sufficient for the exosome-dependent secretion of TG-A. In conclusion, TG-A is secreted through an unconventional ER/Golgi-independent pathway involving two types of fatty acylations and exosomes."xsd:string |
| http://purl.uniprot.org/citations/28476891 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m117.779710"xsd:string |
| http://purl.uniprot.org/citations/28476891 | http://purl.uniprot.org/core/author | "Dong X."xsd:string |
| http://purl.uniprot.org/citations/28476891 | http://purl.uniprot.org/core/author | "Shibata T."xsd:string |
| http://purl.uniprot.org/citations/28476891 | http://purl.uniprot.org/core/author | "Kawasaki D."xsd:string |
| http://purl.uniprot.org/citations/28476891 | http://purl.uniprot.org/core/author | "Kawabata S.I."xsd:string |
| http://purl.uniprot.org/citations/28476891 | http://purl.uniprot.org/core/author | "Hadano J."xsd:string |
| http://purl.uniprot.org/citations/28476891 | http://purl.uniprot.org/core/date | "2017"xsd:gYear |
| http://purl.uniprot.org/citations/28476891 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/28476891 | http://purl.uniprot.org/core/pages | "10723-10734"xsd:string |
| http://purl.uniprot.org/citations/28476891 | http://purl.uniprot.org/core/title | "Drosophila TG-A transglutaminase is secreted via an unconventional Golgi-independent mechanism involving exosomes and two types of fatty acylations."xsd:string |
| http://purl.uniprot.org/citations/28476891 | http://purl.uniprot.org/core/volume | "292"xsd:string |
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