ERK promotes tumorigenesis by inhibiting FOXO3a via MDM2-mediated degradation

By Jer-Yen Yang, C. S. Zong, W. Xia, H. Yamaguchi, Q. Ding, Xiaoming Xie, Jingyu Lang, Chien-Chen Lai, Chun-Ju Chang, Wei‐Chien Huang and 16 more. Nature Cell Biology, 2008

715 citations recorded by the source corpus.

Subfields: Molecular Biology, Pathology and Forensic Medicine

View Paper: https://www.semanticscholar.org/paper/58ea0e26d668a6e1720c1609c69581c394fa2c82

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In Molecular Biology

1. J. Blenis
2. David M. Sabatini
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4. B. Manning

In Pathology and Forensic Medicine

1. J. Blenis

Citations in the corpus

• Glycosylation and stabilization of programmed death ligand-1 suppresses T-cell activity (2016, neutral): “Of note, single protein can be regulated by multiple kinases 31,32 .”
• FoxO transcription factors; Regulation by AKT and 14-3-3 proteins. (2011, background): “The identified E3 ligases for FoxO proteins include SKP2 [128], which binds AKT-phosphorylated FoxO1 at Ser 256 and MDM2, which binds ERK-phosphorylated FoxOs [110,111,129].”
• The Ras-ERK and PI3K-mTOR Pathways: Cross-talk and Compensation (2011, background): “ERK phosphorylates FOXO3A Ser294, Ser344, and Ser425, which increases FOXO3A interaction with the E3ubiquitin ligase MDM2, thereby directing FOXO3A’s ubiquitin-proteasome-mediated degradation [40].”
• Redox regulation of FoxO transcription factors (2015, background): “for murine FoxO1) [66] S294, S344, S425 [65] FoxO1a: enhanced interaction with other transcription factors sug-”