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The NTE domain of PTENα/β promotes cancer progression by interacting with WDR5 via its SSSRRSS motif

Cell Death Dis. 2024-05; 
Xiaolei Huang, Cheng Zhang, Xinci Shang, Yichang Chen, Qin Xiao, Zhengguo Wei, Guanghui Wang, Xuechu Zhen, Guoqiang Xu, Jinrong Min, Shaoming Shen, Yanli Liu
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Proteins, Expression, Isolation and Analysis … Input and IP protein samples were separated on a 4–12% Bis-Tris protein gel (GenScript, M41215C) using Tris-MOPS running buffer and then transferred onto a PVDF membrane and … Get A Quote

摘要

PTENα/β, two variants of PTEN, play a key role in promoting tumor growth by interacting with WDR5 through their N-terminal extensions (NTEs). This interaction facilitates the recruitment of the SET1/MLL methyltransferase complex, resulting in histone H3K4 trimethylation and upregulation of oncogenes such as NOTCH3, which in turn promotes tumor growth. However, the molecular mechanism underlying this interaction has remained elusive. In this study, we determined the first crystal structure of PTENα-NTE in complex with WDR5, which reveals that PTENα utilizes a unique binding motif of a sequence SSSRRSS found in the NTE domain of PTENα/β to specifically bind to the WIN site of WDR5. Disruption of this intera... More

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