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新型核质蛋白 O-岩藻糖基化由 SPINDLY 调控植物中的多种发育过程。

Novel nucleocytoplasmic protein O-fucosylation by SPINDLY regulates diverse developmental processes in plants.

机构信息

Department of Biology, Duke University, Durham, NC 27708, USA.

出版信息

Curr Opin Struct Biol. 2021 Jun;68:113-121. doi: 10.1016/j.sbi.2020.12.013. Epub 2021 Jan 18.

DOI:10.1016/j.sbi.2020.12.013
PMID:33476897
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8222059/
Abstract

In metazoans, protein O-fucosylation of Ser/Thr residues was only found in secreted or cell surface proteins, and this post-translational modification is catalyzed by ER-localized protein O-fucosyltransferases (POFUTs) in the GT65 family. Recently, a novel nucleocytoplasmic POFUT, SPINDLY (SPY), was identified in the reference plant Arabidopsis thaliana to modify nuclear transcription regulators DELLAs, revealing a new regulatory mechanism for gene expression. The paralog of AtSPY, SECRET AGENT (SEC), is an O-link-N-acetylglucosamine (GlcNAc) transferase (OGT), which O-GlcNAcylates Ser/Thr residues of target proteins. Both AtSPY and AtSEC are tetratricopeptide repeat-domain-containing glycosyltransferases in the GT41 family. The discovery that AtSPY is a POFUT clarified decades of miss-classification of AtSPY as an OGT. SPY and SEC play pleiotropic roles in plant development, and the interactions between SPY and SEC are complex. SPY-like genes are conserved in diverse organisms, except in fungi and metazoans, suggesting that O-fucosylation is a common mechanism in modulating intracellular protein functions.

摘要

在后生动物中,丝氨酸/苏氨酸残基的蛋白质 O-连接岩藻糖基化仅在分泌蛋白或细胞表面蛋白中发现,这种翻译后修饰是由内质网定位的 GT65 家族中的蛋白质 O-岩藻糖基转移酶 (POFUT) 催化的。最近,在参考植物拟南芥中鉴定出一种新型核质 POFUT,即 SPINDLY(SPY),它修饰核转录调节剂 DELLAs,揭示了基因表达的新调控机制。AtSPY 的同源物 SECRET AGENT(SEC)是一种 O-连接 N-乙酰葡萄糖胺(GlcNAc)转移酶(OGT),它可以 O-糖基化靶蛋白的丝氨酸/苏氨酸残基。AtSPY 和 AtSEC 都是 GT41 家族中含有四肽重复结构域的糖基转移酶。AtSPY 是 POFUT 的发现澄清了 AtSPY 作为 OGT 的数十年分类错误。SPY 和 SEC 在植物发育中发挥多种作用,SPY 和 SEC 之间的相互作用很复杂。SPY 样基因在不同的生物体中是保守的,除了真菌和后生动物,这表明 O-岩藻糖基化是调节细胞内蛋白质功能的一种常见机制。

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