Inhibition of Wnt signaling by Dishevelled PDZ peptides

被引：133
|
作者：
Zhang, Yingnan [1 ]
Appleton, Brent A. [1 ]
Wiesmann, Christian [1 ]
Lau, Ted [2 ]
Costa, Mike [2 ]
Hannoush, Rami N. [1 ]
Sidhu, Sachdev S. [1 ]
机构：
[1] Genentech Inc, Dept Prot Engn, San Francisco, CA 94080 USA
[2] Genentech Inc, Dept Canc Targets & Pathways, San Francisco, CA 94080 USA
来源：
NATURE CHEMICAL BIOLOGY | 2009年 / 5卷 / 04期
关键词：
BETA-CATENIN; TRANSCRIPTIONAL ACTIVITY; DOMAIN; SPECIFICITY; PATHWAY; OVEREXPRESSION; ANTAGONIST; ACTIVATION; PROTEINS; CANCER;
D O I：
10.1038/nchembio.152
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Dishevelled proteins are key regulators of Wnt signaling pathways that have been implicated in the progression of human cancers. We found that the binding cleft of the Dishevelled PDZ domain is more flexible than those of canonical PDZ domains and enables recognition of both C-terminal and internal peptides. These peptide ligands inhibit Wnt/beta-catenin signaling in cells, showing that Dishevelled PDZ domains are potential targets for small-molecule cancer therapeutics.
引用
收藏
页码：217 / 219
页数：3
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