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https://read.qxmd.com/read/35560335/investigating-the-interaction-of-e6-e6ap-heterodimer-with-p53-dbd-by-fluorescence-resonance-energy-transfer
#1
JOURNAL ARTICLE
Shanna Qu, Yongqi Huang
Human papilloma viruses (HPV) are small DNA viruses, among which the type 16 is the most prevalent and responsible for about 50% of human cervical carcinomas. The E6 oncoprotein of HPV-16 interacts with numerous host proteins by recognizing their LXXLL motifs. One of the HPV-16 E6 cellular binding targets is the E3 ubiquitin ligase E6AP. Once binding, the E6/E6AP heterodimer recruits and ubiquitinates p53, leading to subsequent degradation of p53. Importantly, neither E6 nor E6AP interacts with p53 alone. Therefore, blocking the interaction between E6 and E6AP could stabilize p53...
May 2022: FASEB Journal: Official Publication of the Federation of American Societies for Experimental Biology
https://read.qxmd.com/read/12620801/requirement-of-e6ap-and-the-features-of-human-papillomavirus-e6-necessary-to-support-degradation-of-p53
#2
JOURNAL ARTICLE
Brooke Cooper, Steven Schneider, Joanna Bohl, Yong hui Jiang, Arthur Beaudet, Scott Vande Pol
E6 oncoproteins from human papillomavirus type 16 (16E6) and Bovine Papillomavirus type 1 (BE6) bind to leucine rich peptides (called charged leucine, LXXLL, or signature peptides) found on target cellular proteins. BE6 and 16E6 both bind the product of the UBE3A gene called E6AP on a charged leucine peptide, LQELL. E6AP is an E3 ubiquitin ligase that together with 16E6 interacts with p53 to target p53 degradation. Although both BE6 and 16E6 bind the LQELL peptide of E6AP, only 16E6 acts as an adapter to then bring p53 to E6AP...
February 1, 2003: Virology
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