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Protein kinase A-mediated phosphorylation regulates STAT3 activation and oncogenic EZH2 activity

ABSTRACT: The effect of T372E-EZH2 and Wt-EZH2 overexpression on gene expression in TOV112D cells. We found in this study that Protein Kinase A phosphorylates T372-EZH2 and wanted to determine the gene expression changes brought upon this phosphorylation. We made a point mutation (T372E) that mimicked phospho T372-EZH2. The objective was to observe transcriptional changes in TOV112D cells in response to ectopic expression of Wt-EZH2 and T372E-EZH2 point mutation in TOV112D cells. Overall design: 8 total samples were analyzed 2 for vector control, 2 for Wt-EZH2, 2 for T372A, and 2 for T372E mutation.

INSTRUMENT(S): Illumina NextSeq 500 (Homo sapiens)

SUBMITTER: Kenneth Nephew  

PROVIDER: GSE108418 | GEO | 2018-06-05


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Protein kinase A-mediated phosphorylation regulates STAT3 activation and oncogenic EZH2 activity.

Özeş Ali R AR   Pulliam Nick N   Ertosun Mustafa G MG   Yılmaz Özlem Ö   Tang Jessica J   Çopuroğlu Ece E   Matei Daniela D   Özeş Osman N ON   Nephew Kenneth P KP  

Oncogene 20180326 26

Polycomb repressive complex 2 (PRC2) member enhancer of zeste homolog 2 (EZH2) trimethylates histone H3 lysine 27 (H3K27me3), alters chromatin structure and contributes to epigenetic regulation of gene expression in normal and disease processes. Phosphorylation of EZH2 augmented EZH2 oncogenic activity in cancer but observations have been limited to threonine 350 (T350) and serine 21 (S21) residues by cyclin-dependent kinase 1 and protein kinase B, respectively. In addition, phosphorylation of t  ...[more]

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