Background

Core fucose, a structure added to the reducing end N-acetylglucosamine of N-glycans, has been shown to regulate various physiological and pathological processes, including melanoma metastasis, exacerbation of chronic obstructive pulmonary disease, and severe outcomes in COVID-19.

Scope of review

Recent research has shed light on regulation of the activity and subcellular localization of a1,6-fucosyltransferase (FUT8), the glycosyltransferase responsible for core fucose biosynthesis, unraveling the mechanisms for controlling core fucosylation in vivo.

Major conclusions

This review summarizes the various features of FUT8, including its domains, structures, and substrate specificity. Additionally, we discuss the potential involvement of FUT8-binding proteins, such as oligosaccharyltransferase subunits, in the regulation of FUT8 activity, substrate specificity, and the secretion of FUT8.

General significance

We anticipate that this review will contribute to a deeper understanding of the control of core fucose levels in vivo and involvement of core fucosylation in FUT8-relevant functions and diseases.

中文翻译：

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核心岩藻糖基化酶FUT8的独特结构域和活性调控

背景

核心岩藻糖是一种添加到N-聚糖还原端N-乙酰氨基葡萄糖上的结构，已被证明可以调节各种生理和病理过程，包括黑色素瘤转移、慢性阻塞性肺病的恶化以及 COVID-19 的严重后果。

审查范围

最近的研究揭示了α1,6-岩藻糖基转移酶（FUT8）（负责核心岩藻糖生物合成的糖基转移酶）的活性和亚细胞定位的调节，揭示了体内控制核心岩藻糖基化的机制。

主要结论

本综述总结了 FUT8 的各种特征，包括其域、结构和底物特异性。此外，我们还讨论了 FUT8 结合蛋白（例如寡糖转移酶亚基）在 FUT8 活性、底物特异性和 FUT8 分泌调节中的潜在参与。

一般意义

我们预计本次综述将有助于更深入地了解体内核心岩藻糖水平的控制以及核心岩藻糖基化在 FUT8 相关功能和疾病中的参与。