Regulation of human papillomavirus E6 oncoprotein function via a novel ubiquitin ligase FBXO4.

ABSTRACT: Previous studies have shown that E6 interacts with the E6-associated protein (E6AP) ubiquitin-protein ligase and directs its ubiquitylation activity toward several specific cellular proteins, one of the most important of which is p53. Interestingly, E6AP not only aids in the E6-directed degradation of cellular substrates but also stabilizes the E6 protein by protecting it from proteasome-mediated degradation. However, there is no information available about the ubiquitin ligases that regulate the stability and activity of the human papillomavirus (HPV) E6 oncoprotein in the absence of E6AP. Therefore, to identify these novel ubiquitin ligases, we performed high-throughput human siRNA library screen against ubiquitin ligases in clustered regularly interspaced palindromic repeat (CRISPR)-edi

SUBMITTER: Vats A 

PROVIDER: S-EPMC11796345 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature