Abstract
Ubiquitin-conjugating enzymes (E2 enzymes) such as UBE2T target proteins for degradation via the proteasome. Here, we examined the effects of UBE2T on the progression of gastric cancer. UBE2T was highly expressed in gastric tumors and gastric cancer cells. siRNA-mediated suppression of UBE2T inhibited gastric cancer cell proliferation and colony formation by promoting cell cycle arrest at G2/M phase and increasing apoptosis. Suppression of UBE2T also attenuated the invasive and metastatic abilities of gastric cancer cells by altering expression of epithelial-mesenchymal transition (EMT)-related factors. A xenograft model in which nude mice were injected with UBE2T knockdown human gastric cancer cells confirmed that suppression of UBE2T also decreased tumor formation and growth in vivo. Expression levels of CCND1, Phospho-GSK3B, WNT family members, and MYC were all affected by UBE2T knockdown. These results suggest that UBE2T plays a critical role in gastric cancer, and that it may serve as a useful prognostic biomarker and therapeutic target in gastric cancer patients.
Highlights
Ubiquitination, including both monoubiquitination and polyubiquitination, plays an important role in proteasomemediated the protein degradation
Ubiquitin-conjugating enzyme E2T (UBE2T) was up-regulated in TCGA database gastric carcinoma samples and widely expressed in malignant gastric cancer cells
UBE2T expression was measured in different gastric cancer cell types using real-time PCR
Summary
Ubiquitination, including both monoubiquitination and polyubiquitination, plays an important role in proteasomemediated the protein degradation. The ubiquitination process, which includes activation by ubiquitin-activating enzymes (E1s), conjugation by ubiquitin-conjugating enzymes (E2s), and ligation by ubiquitin ligases (E3s), can alter protein interactions, location, function, activity, and lifespan. Ubiquitin-conjugating enzymes (E2s), which target proteins for degradation via the proteasome, accept ubiquitin from the E1 complex and catalyze monoubiquitination They are involved in mitomycin-C (MMC)-induced DNA repair, the association of Fanconi anemia complex with the E3 ubiquitin-protein ligase FANCL, and catalyzing the monoubiquitination of FANCD2 [3, 4]. They contribute to the ubiquitination and degradation of BRCA1 [5, 6]
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
