CK1ε and p120-catenin control Ror2 function in noncanonical Wnt signaling

Molecular Oncology
Josué CurtoMireia Duñach

Abstract

Canonical and noncanonical Wnt pathways share some common elements but differ in the responses they evoke. Similar to Wnt ligands acting through the canonical pathway, Wnts that activate the noncanonical signaling, such as Wnt5a, promote Disheveled (Dvl) phosphorylation and its binding to the Frizzled (Fz) Wnt receptor complex. The protein kinase CK1ε is required for Dvl/Fz association in both canonical and noncanonical signaling. Here we show that differently to its binding to canonical Wnt receptor complex, CK1ε does not require p120-catenin for the association with the Wnt5a co-receptor Ror2. Wnt5a promotes the formation of the Ror2-Fz complex and enables the activation of Ror2-bound CK1ε by Fz-associated protein phosphatase 2A. Moreover, CK1ε also regulates Ror2 protein levels; CK1ε association stabilizes Ror2, which undergoes lysosomal-dependent degradation in the absence of this kinase. Although p120-catenin is not required for CK1ε association with Ror2, it also participates in this signaling pathway as p120-catenin binds and maintains Ror2 at the plasma membrane; in p120-depleted cells, Ror2 is rapidly internalized through a clathrin-dependent mechanism. Accordingly, downregulation of p120-catenin or CK1ε affects late r...Continue Reading

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Citations

Apr 12, 2019·International Journal of Cancer. Journal International Du Cancer·Enrico MiniStefania Nobili
Mar 17, 2020·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Tianwei HeLimin Rong
Jan 16, 2021·Cells·Kerstin MenckAnnalen Bleckmann

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Methods Mentioned

BETA
GTPases
transfection
PCR
immunoprecipitation
IEC

Software Mentioned

quantity
graphpad prism
GraphPad

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