Peptide Interactions Stabilize and Restructure Human Papillomavirus Type 16 E6 To Interact with p53

被引：42

作者：

Ansari, Tina ^{[1
]}

Brimer, Nicole ^{[1
]}

Vande Pol, Scott B. ^{[1
]}

机构：

[1] Univ Virginia, Dept Pathol, Charlottesville, VA 22903 USA

来源：

JOURNAL OF VIROLOGY | 2012年 / 86卷 / 20期

关键词：

PROTEIN; DEGRADATION; ONCOPROTEIN; ASSOCIATION; UBIQUITINATION; BINDING; IDENTIFICATION; E6-AP; ACTIVATION; ENZYME;

D O I：

10.1128/JVI.01236-12

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Human papillomavirus type 16 (HPV-16) E6 (16E6) binds the E3 ubiquitin ligase E6AP and p53, thereby targeting degradation of p53 (M. Scheffner, B. A. Werness, J. M. Huibregtse, A. J. Levine, and P. M. Howley, Cell 63: 1129 -1136, 1990). Here we show that minimal 16E6-binding LXXLL peptides reshape 16E6 to confer p53 interaction and stabilize 16E6 in vivo but that degradation of p53 by 16E6 requires E6AP expression. These experiments establish a general mechanism for how papillomavirus E6 binding to LXXLL peptides reshapes E6 to then act as an adapter molecule.

引用

页码：11386 / 11391

页数：6

共 27 条

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