PSMD4 regulates the malignancy of esophageal cancer cells by suppressing endoplasmic reticulum stress.

摘要: Proteasome 26S subunit non-ATPase 4 (PSMD4) is an important proteasome ubiquitin receptor and plays a key role in endoplasmic reticulum stress (ERS). However, the study of PSMD4 esophageal cancer (EC) relatively rare. Here, we found that expression was markedly enhanced EC tissues cell lines. The counting kit-8 (CCK-8) assay showed overexpression significantly Eca109 viability, while inhibition reduced viability. Knockdown induced apoptosis cycle arrest. More importantly, knockdown glucose regulated protein 78, activating transcription factor 6, p-protein kinase R-like ER kinase, indicating ERS response cells. Compared with control cells, brefeldin A inhibited increased p53-upregulated modulator apoptosis. such effects were largely reversed after overexpressing suggesting silencing could enhance ERS-induced In summary, upregulation promoted progression mainly by reducing