IndraLab

"These results implied that USP14 promotes the activity of NF-κB and the phosphorylation of ERK1/2 induced by microbial infections (Table 2)."

"These findings suggested that USP14 induces NF-kappaB activity and ERK1/2 phosphorylation triggered by microbial infection."

"In line with our result, genetic or pharmacological inhibition of USP14 led to reduced phosphorylation of Akt and/or Erk1/2 in hepatocellular carcinoma cells and monocytic leukemia cells.25, 26 Moreover, inhibition of PI3K/AKT and ERK1/2 signaling pathways could enhance cisplatin sensitivity in urothelial bladder cancer cells and ovarian cancer cells, respectively.27, 28 As one of three proteasome‐associated DUBs, USP14 plays a key regulatory role in protein proteasomal degradation.29 Inhibition of USP14 activity would lead to a dysfunctional proteasome, eliciting a broad accumulation of ubiquitinated proteins."