O-GlcNAc glycosylation stoichiometry of the FET protein family: only EWS is glycosylated with a high stoichiometry
O-GlcNAc glycosylation stoichiometry of the FET protein family: only EWS is glycosylated with a high stoichiometry
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FET 蛋白家族的 O-GlcNAc 糖基化化学计量：仅 EWS 具有高化学计量糖基化
DOI：
10.1080/09168451.2016.1263148
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发表时间：
2017
期刊：
影响因子：
--
通讯作者：
Kazuo Kamemura
中科院分区：
文献类型：
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作者：
Kawasaki Y;Oda H;Ito J;Niwa A;Tanaka T;Hijikata A;Seki R;Nagahashi A;Osawa M;Asaka I;Watanabe A;Nishimata S;Shirai T;Kawashima H;Ohara O;Nakahata T;Nishikomori R;Heike T;Saito MK.;Kazuo Kamemura
在FET（融合在肉瘤[FUS]/Ewing肉瘤蛋白[EWS]/TATA结合蛋白相关因子15 [TAF15]）异质核核糖-核蛋白颗粒蛋白家族中，FUS和TAF15在神经退行性疾病（如与FUS相关的额颞叶变性）的包涵体中一致存在，而EWS在包涵体中存在差异。据推测，FET蛋白在翻译后水平的失调参与了它们的细胞质沉积。本文对FET蛋白的o -linked β- n -乙酰氨基葡萄糖（O-GlcNAc）糖基化化学计量学进行了化学酶学分析，发现在测试的神经细胞系和小鼠大脑中，只有EWS被动态糖基化并具有高的化学计量学。研究还证实，EWS，而不是FUS和TAF15，不仅在神经细胞中，而且在非神经细胞系中都具有高化学计量量的糖基化。这些结果表明，在大多数细胞系或组织中，o - glcnac糖基化赋予EWS不同于其他FET蛋白的物理化学性质。
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, theO-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 thatO-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.