論文 - 詳細
| RRC ID | 51956 |
|---|---|
| 著者 | Kamemura K. |
| タイトル | O-GlcNAc glycosylation stoichiometry of the FET protein family: only EWS is glycosylated with a high stoichiometry. |
| ジャーナル | Biosci Biotechnol Biochem |
| Abstract |
Of the FET (fused in sarcoma [FUS]/Ewing sarcoma protein [EWS]/TATA binding protein-associated factor 15 [TAF15]) family of heterogeneous nuclear ribonucleoprotein particle proteins, FUS and TAF15 are consistently and EWS variably found in inclusion bodies in neurodegenerative diseases such as frontotemporal lobar degeneration associated with FUS. It is speculated that dysregulation of FET proteins at the post-translational level is involved in their cytoplasmic deposition. Here, the O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation stoichiometry of the FET proteins was chemoenzymatically analyzed, and it was found that only EWS is dynamically glycosylated with a high stoichiometry in the neural cell lines tested and in mouse brain. It was also confirmed that EWS, but not FUS and TAF15, is glycosylated with a high stoichiometry not only in the neural cells but also in the non-neural cell lines tested. These results indicate that O-GlcNAc glycosylation imparts a physicochemical property on EWS that is distinct from that of the other FET proteins in most of cell lineages or tissues. |
| 巻・号 | 81(3) |
| ページ | 541-546 |
| 公開日 | 2017-3-1 |
| DOI | 10.1080/09168451.2016.1263148 |
| PMID | 27903134 |
| MeSH | Acetylglucosamine / metabolism Animals Cell Differentiation Glycosylation Humans Mice Mice, Inbred Strains Neurons / metabolism Neurons / pathology RNA-Binding Protein EWS / chemistry RNA-Binding Protein EWS / metabolism* RNA-Binding Protein FUS / chemistry RNA-Binding Protein FUS / metabolism* TATA-Binding Protein Associated Factors / chemistry TATA-Binding Protein Associated Factors / metabolism* |
| IF | 1.516 |
| 引用数 | 1 |
| オルトメトリクス指標 |
オルトメトリクス指標項目
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| 最多言及媒体 | News |
| 各媒体での言及数の合計 | 1 |
| 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 | A172(RCB2530) |