This entry represents the RNA recognition motif (RRM) of G3BP1, which has been identified as a phosphorylation-dependent endoribonuclease that interacts with the SH3 domain of RasGAP []. However, this interaction has been questioned []. G3BP1 binds to and cleaves the 3'-untranslated region (3'-UTR) of the c-myc mRNA in a phosphorylation-dependent manner []. G3BP1 has been linked to the formation of stress granules (SGs), membrane-less structures consisting of mRNA and protein aggregates form rapidly in response to a wide range of stresses and viral infections [, ]. G3BP1 is targeted by many viruses and may be involved in innate immune response [, ]. Its activities can be regulated through post-translational modifications [].It has also been shown that G3BP1 is a novel Dishevelled-associated protein that is methylated upon Wnt3a stimulation and that arginine methylation of G3BP1 regulates both Ctnnb1 mRNA and canonical Wnt/beta-catenin signaling []. Furthermore, G3BP1 can be associated with the 3'-UTR of beta-F1 mRNA in cytoplasmic RNA-granules, demonstrating that G3BP1 may specifically repress the translation of the transcript [].G3BP1 contains an N-terminal nuclear transfer factor 2 (NTF2)-like domain, an RNA recognition motif (RRM domain), and an Arg-Gly-rich region (RGG-rich region, or arginine methylation motif). The RRM domain and RGG-rich region are canonically associated with RNA binding [].
