国际肿瘤学杂志 ›› 2024, Vol. 51 ›› Issue (12): 769-773.doi: 10.3760/cma.j.cn371439-20240522-00130

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蛋白S-棕榈酰化修饰及其在肿瘤中的作用

谌亮, 李营歌, 郑斯豪, 张偲, 颜琦璐, 宋启斌, 姚颐()   

  1. 武汉大学人民医院肿瘤中心,武汉 430060
  • 收稿日期:2024-05-22 修回日期:2024-06-14 出版日期:2024-12-08 发布日期:2025-01-07
  • 通讯作者: 姚颐 E-mail:yaoyi2018@whu.edu.cn
  • 基金资助:
    湖北省自然科学基金(2022CFB114)

Protein S-palmitoylation and its role in tumor

Chen Liang, Li Yingge, Zheng Sihao, Zhang Cai, Yan Qilu, Song Qibin, Yao Yi()   

  1. Cancer Center, Renmin Hospital of Wuhan University, Wuhan 430060, China
  • Received:2024-05-22 Revised:2024-06-14 Online:2024-12-08 Published:2025-01-07
  • Contact: Yao Yi E-mail:yaoyi2018@whu.edu.cn
  • Supported by:
    National Natural Science Foundation of Hubei Province of China(2022CFB114)

摘要:

蛋白S-棕榈酰化是一种可逆的脂质翻译后修饰,具有调控蛋白定位、稳定性、蛋白间相互作用等功能。棕榈酰转移酶通过催化反应将棕榈酸酯添加至蛋白半胱氨酸残基上,而棕榈酰酯的去除主要通过酰基蛋白硫酯酶的催化。一些肿瘤相关蛋白S-棕榈酰化修饰发生异常改变,并且与肿瘤细胞增殖、侵袭、转移、耐药及肿瘤免疫应答等生物学过程密切相关。进一步探讨蛋白S-棕榈酰化修饰的特点及其在肿瘤进展中的作用,以期为靶向蛋白S-棕榈酰化的肿瘤治疗策略提供新的思路。

关键词: 肿瘤, 蛋白质加工,转译后, S-棕榈酰化, 棕榈酰转移酶, 酰基蛋白硫酯酶

Abstract:

Protein S-palmitoylation is a reversible post-translational modification of lipids that regulates protein localization, stability and protein-protein interactions. The thioesterification of palmitate to internal cysteine residues is catalyzed by palmitoyltransferase, while the removal of palmitate is mainly catalyzed by acyl-protein thioesterase. The S-palmitoylation of some tumor-related proteins is abnormally altered in tumor, which is closely related to the biological processes such as tumor cell proliferation, invasion, metastasis, drug resistance and immune response. Furtherly, exploring the characteristics of protein S-palmitoy-lation and its role in tumor progression could deliver new ideas in targeting protein S-palmitoylation for tumor therapy.

Key words: Neoplasms, Protein processing, post-translational, S-palmitoylation, Palmitoyltransfe-rases, Acyl-protein thioesterases