論文 - 詳細
| RRC ID | 72314 |
|---|---|
| 著者 | Hirata T, Takata M, Tokoro Y, Nakano M, Kizuka Y. |
| タイトル | Shedding of N-acetylglucosaminyltransferase-V is regulated by maturity of cellular N-glycan. |
| ジャーナル | Commun Biol |
| Abstract |
The number of N-glycan branches on glycoproteins is closely related to the development and aggravation of various diseases. Dysregulated formation of the branch produced by N-acetylglucosaminyltransferase-V (GnT-V, also called as MGAT5) promotes cancer growth and malignancy. However, it is largely unknown how the activity of GnT-V in cells is regulated. Here, we discover that the activity of GnT-V in cells is selectively upregulated by changing cellular N-glycans from mature to immature forms. Our glycomic analysis further shows that loss of terminal modifications of N-glycans resulted in an increase in the amount of the GnT-V-produced branch. Mechanistically, shedding (cleavage and extracellular secretion) of GnT-V mediated by signal peptide peptidase-like 3 (SPPL3) protease is greatly inhibited by blocking maturation of cellular N-glycans, resulting in an increased level of GnT-V protein in cells. Alteration of cellular N-glycans hardly impairs expression or localization of SPPL3; instead, SPPL3-mediated shedding of GnT-V is shown to be regulated by N-glycans on GnT-V, suggesting that the level of GnT-V cleavage is regulated by its own N-glycan structures. These findings shed light on a mechanism of secretion-based regulation of GnT-V activity. |
| 巻・号 | 5(1) |
| ページ | 743 |
| 公開日 | 2022-8-1 |
| DOI | 10.1038/s42003-022-03697-y |
| PII | 10.1038/s42003-022-03697-y |
| PMID | 35915223 |
| PMC | PMC9343384 |
| MeSH | Cell Line, Tumor Glycoproteins / chemistry N-Acetylglucosaminyltransferases* / genetics N-Acetylglucosaminyltransferases* / metabolism Polysaccharides* / metabolism |
| IF | 4.165 |
| オルトメトリクス指標 |
オルトメトリクス指標項目
|
| 最多言及媒体 | News |
| 各媒体での言及数の合計 | 8 |
| 過去6か月間でのオルトメトリクス指標の変動値 | 0.0 |
| リソース情報 | |
| ヒト・動物細胞 | COS-7(RCB0539) B16 |