Arginine methylation of G3BP1 in response to Wnt3a regulates β-catenin mRNA | Zendy

Rama Kamesh Bikkavilli | Zendy; Craig C. Malbon | Zendy

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Arginine methylation of G3BP1 in response to Wnt3a regulates β-catenin mRNA

Author(s) -

Rama Kamesh Bikkavilli,

Craig C. Malbon

Publication year - 2011

Publication title -

journal of cell science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.384

H-Index - 278

eISSN - 1477-9137

pISSN - 0021-9533

DOI - 10.1242/jcs.084046

Subject(s) - biology , wnt3a , dishevelled , methylation , wnt signaling pathway , protein arginine methyltransferase 5 , arginine , microbiology and biotechnology , phosphoprotein , messenger rna , frizzled , signal transduction , phosphorylation , biochemistry , amino acid , gene , methyltransferase

Wnt/β-catenin signaling is essential for normal mammalian development. Wnt3a activates the Wnt/β-catenin pathway through stabilization of β-catenin; a process in which the phosphoprotein Dishevelled figures prominently. Protein arginine methylation in signaling complexes containing Dishevelled was investigated. Mass spectrometry of a prominent arginine-methylated, Dishevelled-associated protein identified the Ras GTPase activating protein-binding protein 1 G3BP1. Stimulation of totipotent mouse embryonic F9 cells with Wnt3a provoked increased methylation of G3BP1. We show that G3BP1 is a novel Ctnnb1 mRNA binding protein. Methylation of G3BP1 constitutes a molecular switch that regulates Ctnnb1 mRNA in response to Wnt3a. Thus, the protein arginine methylation that targets G3BP1 acts as a novel regulator of Ctnnb1 mRNA.

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