国际妇产科学杂志 ›› 2021, Vol. 48 ›› Issue (2): 121-125.doi: 10.12280/gjfckx.20200596

• 妇科肿瘤研究 综述 •    下一篇

E3泛素连接酶CUL2在宫颈癌中的研究进展

张宏蕾, 赵卫红()   

  1. 030001太原,山西医科大学基础医学院(张宏蕾);山西医科大学第二医院妇产科(赵卫红)
  • 收稿日期:2020-07-08 出版日期:2021-04-15 发布日期:2021-04-16
  • 通讯作者: 赵卫红 E-mail:sydeyzwh@sxmu.edu.cn
  • 基金资助:
    国家自然科学基金(81702583);山西省优秀青年基金(201901D211506)

Research Progress of E3 Ubiquitin Ligase CUL2 in Cervical Cancer

ZHANG Hong-lei, ZHAO Wei-hong()   

  1. Basic Medical College, Shanxi Medical University, Taiyuan 030001, China (ZHANG Hong-lei) ; Department of Obstetrics and Gynecology, Second Hospital of Shanxi Medical University, Taiyuan 030001, China (ZHAO Wei-hong)
  • Received:2020-07-08 Published:2021-04-15 Online:2021-04-16
  • Contact: ZHAO Wei-hong E-mail:sydeyzwh@sxmu.edu.cn

摘要:

泛素化是蛋白质翻译后调控的重要途径。作为体内最大的 E3 泛素连接酶家族,Cullin-Ring类E3泛素连接酶广泛参与调控机体内细胞周期蛋白和转录因子的降解。其中,CUL2作为骨架分子形成CUL2泛素连接酶复合物,在希佩尔-林道(von Hippel-Lindau, VHL)肿瘤抑制因子相关受体底物的泛素化降解中发挥重要的作用。目前,研究发现CUL2普遍参与肿瘤血管生成、细胞动力、免疫逃逸、细胞增殖及等肿瘤恶变机制的调控。综述CUL2在肿瘤发生中的作用机制及其与宫颈癌的关系,旨在为宫颈癌的诊断和治疗提供新的作用靶点。

关键词: 宫颈肿瘤, 癌, 泛素蛋白连接酶类, 泛素化蛋白, 泛素化, 脑视网膜血管瘤抑制蛋白质

Abstract:

Ubiquitin is an important way of post-translational regulation of proteins. As the largest E3 ubiquitin ligase family in vivo, Cullin-Ring E3 ubiquitin ligases are widely involved in regulating the degradation of cyclins and transcription factors in vivo. CUL2, as a skeleton molecule, forms the CUL2 ubiquitin ligase complex, which plays an important role in the ubiquitination degradation of von Hippel-Lindau (VHL) tumor suppressor related receptor substrates. At present, studies have found that CUL2 is generally involved in the regulation of tumor malignant transformation mechanisms such as tumor angiogenesis, cell dynamics, immune escape, cell proliferation, and epithelial mesenchymal transition. In this paper, the mechanism of CUL2 in carcinogenesis and its relationship with cervical cancer are reviewed, aiming to provide a new target for diagnosis and treatment of cervical cancer.

Key words: Uterine cervical neoplasms, Carcinoma, Ubiquitin-protein ligases, Ubiquitinated proteins, Ubiquitination, Von hippel-lindau tumor suppressor protein