Phosphorylated DVL recruits PIP5K1B to the plasma membrane

Stable Identifier
Reaction [binding]
Homo sapiens
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DVL1 and 3 have been shown to co-immunoprecipitate with PIP5KB in HEK293 cells. This interaction is mediated by the N-terminal half of the kinase and the PDZ and DIX domain of DVL and recruits PIPK5B to the receptor complex. The interaction of DVL and PIP5KB is required for the WNT3A-dependent phosphorylation of LRP6 at serine 1490 and threonine 1479, as well as and the subsequent formation of the signalosome and recruitment of AXIN (Pan et al, 2008).

Literature References
PubMed ID Title Journal Year
18772438 Wnt3a-mediated formation of phosphatidylinositol 4,5-bisphosphate regulates LRP6 phosphorylation

Pan, W, Choi, SC, Wang, H, Qin, Y, Volpicelli-Daley, L, Swan, L, Lucast, L, Khoo, C, Zhang, X, Li, L, Abrams, CS, Sokol, SY, Wu, D

Science 2008
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Orthologous Events
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