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Wnt3a-stimulated LRP6 phosphorylation is dependent upon arginine methylation of G3BP2
Rama Kamesh Bikkavilli, Craig C. Malbon


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–β-catenin signaling.


  • * Present address: Division of Pulmonary Sciences and Critical Care, School of Medicine, Anschutz Medical Campus, University of Colorado Health Sciences Center, Denver, Colorado 80045, USA

  • Funding

    This work was supported by US Public Health Service Grant from the National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health [grant number DK30111 to C.C.M.). Deposited in PMC for immediate release.

  • Supplementary material available online at

  • Accepted January 16, 2012.

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