- VernacularTitle:去泛素化酶USP28在肿瘤中的作用及其抑制剂研究进展
- Author:
Xing LI
1
,
2
;
Bo-ya ZHANG
1
,
2
;
Li-ting LU
1
,
2
;
Yan WANG
1
,
2
;
Shuai WEN
1
,
2
;
Yong-jun ZANG
3
;
Xiang-ming XU
1
,
2
;
Yi MOU
1
,
2
Author Information
- Publication Type:Research Article
- Keywords: eubiquitylating enzyme; ubiquitin-specific protease 28; cancer; inhibitor; ubiquitination
- From: Acta Pharmaceutica Sinica 2024;59(11):2941-2952
- CountryChina
- Language:Chinese
- Abstract: The deubiquitinases (DUBs), as the crucial peptidohydrolases in the ubiquitin system, can reverse and strictly regulate ubiquitination and play key roles in various biological processes, including the regulation of protein stability, cell signal transduction. Ubiquitin-specific protease 28 (USP28) involves multiple cancer-related signaling pathways by enhancing the stability of various cancer-related proteins, and is closely associated with the progression of colorectal, breast cancer, lung carcinomas, and pancreatic cancer. USP28 has been considered as a promising drug target in anticancer therapy, and the development of USP28 inhibitors has made some progress. In this article, we review the structure of USP28 and its interaction with substrates, discuss the research progress of USP28 in cancers and summarize the development of USP28 inhibitors.