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- W2615385974 abstract "The scaffold protein Dishevelled is a central intracellular component of Wnt signaling pathways. Various kinases have been described that regulate and modulate Wnt signaling through phosphorylation of Dishevelled. However, besides the general protein phosphatases 1 and 2 (PP1 and PP2), no specific protein phosphatases have been identified. Here, we report on the identification and functional characterization of the protein phosphatase Pgam5 in vitro and in vivo. Pgam5 is a novel antagonist of Wnt/β-Catenin signaling in human cells and Xenopus embryogenesis. In early development, Pgam5 is essential for head formation and establishing and maintaining the Wnt/β-Catenin signaling gradient that patterns the anterior-posterior body axis. Inhibition of Wnt/β-Catenin signaling and developmental function depend on Pgam5 phosphatase activity. We show that Pgam5 interacts with Dishevelled2 and that Dishevelled2 is a substrate of Pgam5. Pgam5 mediates a marked decrease of Dishevelled2 phosphorylation in the cytoplasm and in the nucleus as well as decreased interaction between Dishevelled2, Tcf1 and β-Catenin, indicating that Pgam5 regulates Dishevelled function upstream and downstream of β-Catenin stabilization." @default.
- W2615385974 created "2017-05-26" @default.
- W2615385974 creator A5017491987 @default.
- W2615385974 creator A5018625809 @default.
- W2615385974 creator A5030365012 @default.
- W2615385974 creator A5036143602 @default.
- W2615385974 creator A5042581403 @default.
- W2615385974 creator A5050876763 @default.
- W2615385974 creator A5057753238 @default.
- W2615385974 creator A5060574898 @default.
- W2615385974 date "2017-01-01" @default.
- W2615385974 modified "2023-09-24" @default.
- W2615385974 title "The phosphatase Pgam5 antagonizes Wnt/β-Catenin signaling in embryonic anterior-posterior axis patterning" @default.
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- W2615385974 doi "https://doi.org/10.1242/dev.144477" @default.