Interaction of FAM5C with UDP-glucose:glycoprotein glucosyltransferase 1 (UGGT1): Implication of N -glycosylation in FAM5C secretion
| Autor: | Hidenobu Fujita, Yuya Terao, Junya Sato, Yoshiyuki Rikitake, Miwako Kobayashi, Sayo Horibe, Seimi Satomi-Kobayashi, Ichiro Matsuoka, Naoto Sasaki, Satomi Minami, Ken-ichi Hirata |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Protein Folding Glycosylation Leukocyte adhesion molecule Biophysics Gene Expression Biology Endoplasmic Reticulum Biochemistry 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine N-linked glycosylation Humans Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Secretion Molecular Biology chemistry.chemical_classification Tunicamycin Endoplasmic reticulum Cell Biology Cell biology DNA-Binding Proteins carbohydrates (lipids) HEK293 Cells 030104 developmental biology chemistry Glucosyltransferases Mutation biology.protein Tumor necrosis factor alpha Glucosyltransferase Asparagine Glycoprotein Protein Processing Post-Translational 030217 neurology & neurosurgery |
| Zdroj: | Biochemical and Biophysical Research Communications. 486:811-816 |
| ISSN: | 0006-291X |
| Popis: | N-glycosylation of proteins is important for protein folding and function. We have recently reported that FAM5C/BRINP3 contributes to the tumor necrosis factor-α-induced expression of leukocyte adhesion molecules in vascular endothelial cells (ECs). However, regulatory mechanism of the FAM5C biosynthesis is poorly understood. Co-immunoprecipitation assay revealed the interaction of FAM5C with UDP-glucose:glycoprotein glucosyltransferase 1 (UGGT1), a glycoprotein folding-sensor enzyme. FAM5C ectopically expressed in HEK293 cells was localized to the endoplasmic reticulum and co-localized with endogenously expressed UGGT1. Molecular size of FAM5C was reduced by treatment with N-glycosidase F and in FAM5C-expressing cells cultured in the presence of the N-glycosylation inhibitor tunicamycin. FAM5C was secreted by the cells and the secretion of FAM5C was blocked by tunicamycin. Among six potential N-glycosylation sites, the potential site at Asn168 was not N-glycosylated, and Asn337, Asn456, Asn562, Asn609, and Asn641 mutants were poorly secreted by the cells. These results demonstrated that FAM5C is an N-glycosylated protein and N-glycosylation is necessary for the secretion of FAM5C. |
| Databáze: | OpenAIRE |
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