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Publication : Wnt3a-stimulated LRP6 phosphorylation is dependent upon arginine methylation of G3BP2.

First Author  Bikkavilli RK Year  2012
Journal  J Cell Sci Volume  125
Issue  Pt 10 Pages  2446-56
PubMed ID  22357953 Mgi Jnum  J:197712
Mgi Id  MGI:5494366 Doi  10.1242/jcs.100933
Citation  Bikkavilli RK, et al. (2012) Wnt3a-stimulated LRP6 phosphorylation is dependent upon arginine methylation of G3BP2. J Cell Sci 125(Pt 10):2446-56
abstractText  Wnt signaling is initiated upon binding of Wnt proteins to Frizzled proteins and their co-receptors LRP5 and 6. The signal is then propagated to several downstream effectors, mediated by the phosphoprotein scaffold, dishevelled. We report a novel role for arginine methylation in regulating Wnt3a-stimulated LRP6 phosphorylation. G3BP2, a dishevelled-associated protein, is methylated in response to Wnt3a. The Wnt3a-induced LRP6 phosphorylation is attenuated by G3BP2 knockdown, chemical inhibition of methyl transferase activity or expression of methylation-deficient mutants of G3BP2. Arginine methylation of G3BP2 appears to be a Wnt3a-sensitive 'switch' regulating LRP6 phosphorylation and canonical Wnt-beta-catenin signaling.
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