利用质谱法蛋白质组学策略破译蛋白质长链s -酰化。

IF 3.1 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY
Anneroos E. Nederstigt, Samiksha Sardana and Marc P. Baggelaar
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引用次数: 0

摘要

蛋白质长链s酰化是脂肪酸(如棕榈酸酯)通过硫酯键与半胱氨酸残基的可逆连接,是一种广泛存在的翻译后修饰,在调节蛋白质定位、运输和稳定性方面起着至关重要的作用。尽管长链s -酰化具有普遍性和生物学相关性,但由于脂质修饰的疏水性和不稳定性,使传统的蛋白质组学工作流程复杂化,长链s -酰化的研究长期落后于其他动态PTMs。基于质谱的策略的最新进展大大扩展了研究长链s -酰化的工具箱,改进了工作流程,使分析更加敏感、位点特异性和定量。本文综述了过去十年来基于直接和间接质谱的策略的主要进展,包括酰基生物素交换、脂质代谢标记和新的富集和碎片化方法。我们还强调了在区分脂质特异性修饰,实现稳健的量化和减轻体外系统的伪像方面出现的新挑战,同时概述了未来的方向,以推进s -酰基(蛋白质)组的功能和治疗探索。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Deciphering protein long-chain S-acylation using mass spectrometry proteomics strategies

Deciphering protein long-chain S-acylation using mass spectrometry proteomics strategies

Protein long-chain S-acylation, the reversible attachment of fatty acids such as palmitate to cysteine residues via thioester bonds, is a widespread post-translational modification that plays a crucial role in regulating protein localization, trafficking, and stability. Despite its prevalence and biological relevance, the study of long-chain S-acylation has long lagged behind that of other dynamic PTMs due to the hydrophobic nature and lability of the lipid modification, which complicate conventional proteomic workflows. Recent advances in mass spectrometry-based strategies have significantly expanded the toolbox for studying long-chain S-acylation, with improved workflows enabling more sensitive, site-specific, and quantitative analysis. This review summarizes key developments from the past decade across both direct and indirect mass spectrometry-based strategies, including acyl-biotin exchange, lipid metabolic labeling, and novel enrichment and fragmentation methods. We also highlight emerging challenges in distinguishing lipid-specific modifications, achieving robust quantification, and mitigating artifacts from in vitro systems, while outlining future directions to advance functional and therapeutic exploration of the S-acyl-(prote)ome.

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来源期刊
CiteScore
6.10
自引率
0.00%
发文量
128
审稿时长
10 weeks
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