Proximity labeling technologies to illuminate glycan-protein interactions.

Proximity labeling technologies to illuminate glycan-protein interactions.
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邻近标记技术阐明聚糖-蛋白质相互作用。

DOI:
10.1016/j.cbpa.2022.102233
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发表时间:
2023
影响因子:
7.8
通讯作者:
Huang,MiaL
Huang,MiaL
中科院分区:
生物学2区
文献类型:
--
作者:
Reeves,AbigailE;Huang,MiaL

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糖基化是一种普遍存在的翻译后修饰,由糖结合蛋白(GBP)读取以编码重要功能,但对这些相互作用及其后果的深入理解可能是一项具有挑战性的发现。糖-GBP的相互作用是短暂的和微弱的,这使得它们很难被捕获,而糖基化是动态的和异质性的,有必要在天然细胞环境中进行研究来确定内源配体。邻近标记是一种将生物分子标记在目标蛋白质附近的实验性创新,最近已成为克服这些限制的一种强有力的策略,允许在细胞中标记相互作用子,以便随后通过基于质谱学的蛋白质组学进行浓缩和鉴定。我们将描述这项新技术,并在过去五年中与不同的GBP类别讨论它的应用,包括Siglecs、Galectins和非人类凝集素。
Glycosylation is a ubiquitous post-translational modification read by glycan-binding proteins (GBP) to encode important functions, but a robust understanding of these interactions and their consequences can be challenging to uncover. Glycan-GBP interactions are transient and weak, making them difficult to capture, and glycosylation is dynamic and heterogenous, necessitating study in native cellular environments to identify endogenous ligands. Proximity labeling, an experimental innovation that labels biomolecules close to a protein of interest, has recently emerged as a powerful strategy to overcome these limitations, allowing interactors to be tagged in cells for subsequent enrichment and identification by mass spectrometry-based proteomics. We will describe this nascent technique and discuss its applications in the last five years with different GBP classes, including Siglecs, galectins, and non-human lectins.
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