期刊
ONCOTARGET
卷 7, 期 29, 页码 46707-46716出版社
IMPACT JOURNALS LLC
DOI: 10.18632/oncotarget.8732
关键词
cullin-ring ligase(CRL); cullin2; E3 ligase; substrate recognition subunit (SRS)
资金
- Natural Science Foundation for High Education of Jiangsu Province [13KJB320010]
- Jiangsu Provincial Special Program of Medical Science [BL2012030]
- Jiangsu province ordinary university graduate student research innovation project [CXLX13_571]
- Natural Science Foundation of China [81372321, 81201830, 81472200, 81501977]
The Cullin2-type ubiquitin ligases belong to the Cullin-Ring Ligase (CRL) family, which is a crucial determinant of proteasome-based degradation processes in eukaryotes. Because of the finding of von Hippel-Lindau tumor suppressor (VHL), the Cullin2-type ubiquitin ligases gain focusing in the research of many diseases, especially in tumors. These multisubunit enzymes are composed of the Ring finger protein, the Cullin2 scaffold protein, the Elongin B&C linker protein and the variant substrate recognition subunits (SRSs), among which the Cullin2 scaffold protein is the determining factor of the enzyme mechanism. Substrate recognition of Cullin2-type ubiquitin ligases depends on SRSs and results in the degradation of diseases associated substrates by intracellular signaling events. This review focuses on the diversity and the multifunctionality of SRSs in the Cullin2-type ubiquitin ligases, including VHL, LRR-1, FEM1b, PRAME and ZYG11. Recently, as more SRSs are being discovered and more aspects of substrate recognition have been illuminated, insight into the relationship between Cul2-dependent SRSs and substrates provides a new area for cancer research.
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