Chemical reporters for exploring protein acylation.
Chemical reporters for exploring protein acylation.
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DOI：
10.1042/bst20150004
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发表时间：
2015-04
影响因子：
3.9
通讯作者：
Hang HC
中科院分区：
文献类型：
--
作者：
Thinon E;Hang HC
蛋白质被各种代谢物酰化，这些代谢物调节所有生命王国中的许多重要细胞途径。细胞中的酰基在结构上可以从最小的单元乙酸酯变化到修饰的长链脂肪酸，所有这些都可以被激活并共价连接到不同的氨基酸侧链，从而调节蛋白质功能。例如，赖氨酸残基的乙酰化可以改变蛋白质的电荷状态，并产生新的识别元件用于蛋白质-蛋白质相互作用。或者，长链脂肪酰化将蛋白质靶向至膜，并使得能够空间控制细胞信号传导。为了促进生物学中蛋白质酰化的分析，已经开发了带有炔或叠氮化物标签的酰基类似物，其能够使用生物正交连接方法对修饰的蛋白质进行荧光成像和蛋白质组学分析。在此，我们总结了目前可用的酰化化学报告，并强调其效用，发现和量化蛋白质酰化在生物学中的作用。
Proteins are acylated by a variety of metabolites that regulates many important cellular pathways in all kingdoms of life. Acyl groups in cells can vary in structure from the smallest unit, acetate, to modified long chain fatty acids, all of which can be activated and covalently attached to diverse amino acid side chains and consequently modulate protein function. For example, acetylation of Lys residues can alter the charge state of proteins and generate new recognition elements for protein–protein interactions. Alternatively, long chain fatty-acylation targets proteins to membranes and enables spatial control of cell signalling. To facilitate the analysis of protein acylation in biology, acyl analogues bearing alkyne or azide tags have been developed that enable fluorescent imaging and proteomic profiling of modified proteins using bioorthogonal ligation methods. Herein, we summarize the currently available acylation chemical reporters and highlight their utility to discover and quantify the roles of protein acylation in biology.