PP1A-Mediated Dephosphorylation Positively Regulates YAP2 Activity
Author Information
Author(s): Wang Pei, Bai Yujie, Song Bangrong, Wang Yadong, Liu Dong, Lai Yongqiang, Bi Xiaolin, Yuan Zengqiang
Primary Institution: State Key Laboratory of Brain and Cognitive Sciences, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China
Hypothesis
PP1A interacts with and dephosphorylates YAP2, affecting its nuclear accumulation and transcriptional activity.
Conclusion
PP1A-mediated dephosphorylation enhances YAP2's transcriptional activity and pro-survival capability in ovarian cancer cells.
Supporting Evidence
- PP1A interacts with YAP2 in both cytoplasmic and nuclear fractions.
- PP1A dephosphorylates YAP2 at serine 127, leading to its nuclear accumulation.
- Inhibition of PP1A reduces YAP2's transcriptional activity.
- YAP2 expression protects ovarian cancer cells from cisplatin-induced cell death.
Takeaway
This study shows that a protein called PP1A helps another protein, YAP2, work better by removing a chemical tag that usually keeps YAP2 from doing its job in the cell.
Methodology
The study involved biochemical purification, in vitro kinase assays, and luciferase reporter assays to analyze the interaction and effects of PP1A on YAP2.
Statistical Information
P-Value
p<0.05
Statistical Significance
p<0.05
Digital Object Identifier (DOI)
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