West China Second University Hospital, State Key Laboratory of Biotherapy, and Key Laboratory of Birth Defects and Related Diseases of Women and Children, Ministry of Education, Sichuan University, 610041, Chengdu, China.
Department of Neurosurgery, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University and The Research Units of West China, Chinese Academy of Medical Sciences, Chengdu, China.
Cell Death Dis. 2021 Jul 14;12(7):703. doi: 10.1038/s41419-021-03987-z.
Lysine crotonylation has been discovered in histone and non-histone proteins and found to be involved in diverse diseases and biological processes, such as neuropsychiatric disease, carcinogenesis, spermatogenesis, tissue injury, and inflammation. The unique carbon-carbon π-bond structure indicates that lysine crotonylation may use distinct regulatory mechanisms from the widely studied other types of lysine acylation. In this review, we discussed the regulation of lysine crotonylation by enzymatic and non-enzymatic mechanisms, the recognition of substrate proteins, the physiological functions of lysine crotonylation and its cross-talk with other types of modification. The tools and methods for prediction and detection of lysine crotonylation were also described.
赖氨酸丁酰化已在组蛋白和非组蛋白中被发现，并被发现参与多种疾病和生物学过程，如神经精神疾病、致癌作用、精子发生、组织损伤和炎症。独特的碳-碳π键结构表明，赖氨酸丁酰化可能使用与广泛研究的其他类型的赖氨酸酰化不同的调节机制。在这篇综述中，我们讨论了酶和非酶机制对赖氨酸丁酰化的调节、底物蛋白的识别、赖氨酸丁酰化的生理功能及其与其他类型修饰的相互作用。还描述了赖氨酸丁酰化的预测和检测工具和方法。
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