IndraLab

Statements


| 6

sparser
"We identify USP48 as a novel upstream regulator of HEG1: USP48 binds directly to HEG1 and selectively removes K48-linked polyubiquitin chains, thereby abrogating proteasomal degradation and reinforcing HEG1’s oncogenic activity."

sparser
"HEG1 interacts with USP48 and is positively regulated by USP48 in STAD."

sparser
"We found that USP48 binds to HEG1, and the level of HEG1 protein decreases after USP48 is knocked down."

sparser
"Overall, our findings propose a novel USP48HEG1 axis in gastric cancer and provide a foundation for future investigations into the biological functions of HEG1 stabilization and the potential of USP48 as a therapeutic target."

sparser
"To investigate the functional interaction between USP48 and HEG1 in the progression of gastric cancer, we first established USP48 knockdown models in SGC-7901 and AGS cells."

sparser
"Furthermore, our study demonstrates that HEG1 physically interacts with USP48 and is positively regulated by this deubiquitinase."