Unknown kinase phosphorylates p-DVL

Stable Identifier
Reaction [transition]
Homo sapiens
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In response to WNT signaling, dishevelled (DVL) proteins are phosphorylated within the C-terminus. This site appears to be common for both canonical and non-canonical WNT signaling as a similar phosphorylation pattern is observed upon stimulation with WNT1 and WNT5A and no discernable supershifted phosphoform is detected upon simultaneous treatment with both ligands (Gonzalez-Sancho et al, 2004). The kinase responsible for this phosphorylation has not been identified, although CK2, CK1 delta and epsilon and PAR1 have all been shown to phosphorylate DVL in vitro and in vivo under varying conditions (reviewed in Gao and Chen, 2010). WNT3a or WNT5a-induced phosphorylation sites are Ser594, Thr595 and Ser597 in Dvl2 (Gonzalez-Sancho et al. 2013).
Literature References
PubMed ID Title Journal Year
20006983 Dishevelled: The hub of Wnt signaling

Chen, YG, Gao, C

Cell. Signal. 2010
23396967 Functional consequences of Wnt-induced dishevelled 2 phosphorylation in canonical and noncanonical Wnt signaling

Baljinnyam, B, Lee, KH, González-Sancho, JM, Takigawa, Y, Brown, AM, Lee, KS, Greer, YE, Abrahams, CL, Rubin, JS

J. Biol. Chem. 2013
15143170 Wnt proteins induce dishevelled phosphorylation via an LRP5/6- independent mechanism, irrespective of their ability to stabilize beta-catenin

Brennan, KR, González-Sancho, JM, Brown, AM, Castelo-Soccio, LA

Mol. Cell. Biol. 2004
Catalyst Activity

protein serine/threonine kinase activity of unknown kinase [cytosol]

Inferred From
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