Title : Deubiquitylase USP31 induces autophagy and promotes the progression in lung squamous cell carcinoma cells by stabilizing E2F1 expression
Abstract:
Autophagy exerts a vital role in lung squamous cell carcinoma (LUSC) progression. Ubiquitin Specific Peptidase 31 (USP31) has recently been found to be involved in the development of a variety of cancers. However, whether USP31 modulates autophagy in LUSC remains uncovered. This study revealed that high level of USP31 was discovered in LUSC tissue samples employing Gene Expression Profiling Interactive Analysis (GEPIA) database, quantitative real time PCR (qRT-PCR) and immunoblotting analyses. Cell proliferation was tested via cell counting kit 8 (CCK-8) as well as colony formation, which proved USP31 depletion reduced cell viability. Immunofluorescence assay illustrated that USP31 knockdown blocked the occurrence of autophagy in LUSC cells. Meanwhile, USP31 was confirmed to stabilize the expression of E2F1 by proteasome pathway. Furthermore, overexpressed E2F1 effectively eliminated the effects of USP31 knockdown on proliferation and autophagy of LUSC cells. In summary, this investigation proved that USP31 promoted growth and autophagy in LUSC cells at least partly by stabilizing E2F1 expression, which provided a potential therapeutic gene for treating LUSC.
Audience Take Away Notes:
- Ubiquitin Specific Peptidase 31 (USP31) facilitates proliferation of lung squamous cell carcinoma (LUSC) cells
- USP31 depletion inhibits autophagy in LUSC cells
- USP31 induces autophagy by stabilizing the protein level of E2F1
- USP31 could be a potential therapeutic gene for treating LUSC
