Journal
MOLECULAR BIOTECHNOLOGY
Volume -, Issue -, Pages -Publisher
SPRINGERNATURE
DOI: 10.1007/s12033-023-00814-y
Keywords
Apoptosis; Deubiquitinase; Proteolysis; Knockout; Oncogenic transformation; Ubiquitination
Ask authors/readers for more resources
In this study, USP19 is identified as a negative regulator of p53 protein level in cervical cancer progression. The direct interaction between USP19 and p53 is demonstrated by pull down assay. Overexpression of USP19 promotes ubiquitination of p53 and reduces its protein half-life. CRISPR/Cas9-mediated knockout of USP19 elevates p53 protein levels, resulting in reduced colony formation, cell migration, and cell invasion in cervical cancer cells.
p53 is a tumor suppressor gene activated in response to cellular stressors that inhibits cell cycle progression and induces pro-apoptotic signaling. The protein level of p53 is well balanced by the action of several E3 ligases and deubiquitinating enzymes (DUBs). Several DUBs have been reported to negatively regulate and promote p53 degradation in tumors. In this study, we identified USP19 as a negative regulator of p53 protein level. We demonstrate a direct interaction between USP19 and p53 by pull down assay. The overexpression of USP19 promoted ubiquitination of p53 and reduced its protein half-life. We also demonstrate that CRISPR/Cas9-mediated knockout of USP19 in cervical cancer cells elevates p53 protein levels, resulting in reduced colony formation, cell migration, and cell invasion. Overall, our results indicate that USP19 negatively regulates p53 protein levels in cervical cancer progression.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available