DVL2 is phosphorylated after WNT5A binding to FZD

Stable Identifier
Reaction [transition]
Homo sapiens
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DVL2 is phosphorylated upon WNT5A stimulation of HEK293 cells. In human mammary carcinoma cells, DVL2 has been shown to be constititutively bound to PARD6A, irrespective of WNT stimulation and DVL phosphorylation (Narimatsu et al, 2009). PARD6A is a partitioning protein with known roles in the establishment of apico-basal polarity (reviewed in Chen and Zhang, 2013). More recently, PARD6A and the SMURF ubiquitin ligases have been implicated in the PCP pathway, targeting the core PCP protein Prickle1 for degradation (Narimatsu et al, 2009). WNT5A-dependent phosphorylation of DVL2 is required for the subsequent recruitment of SMURF1/2 ubiquitin ligases to the DVL2-PARD6A complex (Narimatsu et al, 2009)

Literature References
PubMed ID Title Journal Year
23535009 The Par3/Par6/aPKC complex and epithelial cell polarity

Chen, J, Zhang, M

Exp. Cell Res. 2013
19379695 Regulation of planar cell polarity by Smurf ubiquitin ligases

Narimatsu, M, Bose, R, Pye, M, Zhang, L, Miller, B, Ching, P, Sakuma, R, Luga, V, Roncari, L, Attisano, L, Wrana, JL

Cell 2009
Participant Of
Catalyst Activity
Catalyst Activity
protein serine/threonine kinase activity of unknown kinase [cytosol]
Physical Entity
This event is regulated
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