anti-GTPase Activating Protein (SH3 Domain) Binding Protein 1 (G3BP1) Antibodies

Human GTPase Activating Protein (SH3 Domain) Binding Protein 1 (G3BP1) interaction partners

1. data reveal G3BP1 as a critical component of RIG-I signaling and possibly acting as a co-sensor to promote RIG-I recognition of pathogenic RNA.

2. Study demonstrated that the cytosolic lncRNA P53RRA is downregulated in cancers and functions as a tumor suppressor by inhibiting cancer progression. P53RRA bound G3BP1 and cytosolic P53RRA-G3BP1 interaction displaced p53 from a G3BP1 complex, resulting in greater p53 retention in the nucleus, which led to cell-cycle arrest, apoptosis, and ferroptosis.

3. this paper shows that G3BP1 promotes DNA binding and activation of cyclic GMP-AMP synthase

4. Ras GTPase-activating protein SH3-domain-binding protein (G3BP1) shows alternating binding in nanocores and anomalous diffusion in the liquid phase of stress granules.

5. High G3BP1expression is associated with arteriosclerosis.

6. The disruption of stress granules (SGs) during the late stage of Enterovirus 71 (EV71) infection is caused by viral protease 3C-mediated cleavage of G3BP stress granule assembly factor 1 (G3BP1). Over-expression of G3BP1-SGs negatively impacts viral replication at the cytopathic effect (CPE), protein, RNA, and viral titer levels.

7. JMJD6 is a novel Stress Granule component that interacts with G3BP1 complexes, and its expression reduces G3BP1 monomethylation and asymmetric dimethylation at three Arg residues.

8. Activated glucocorticoid receptor induced phosphorylation of v-AKT Murine Thymoma Viral Oncogene Homologue (AKT) kinase, which in turn phosphorylated and promoted nuclear translocation of G3BP1. The nuclear G3BP1 bound to the G3BP1 consensus sequence located on primary miR-15b~16-2 and miR-23a~27a~24-2 to inhibit their maturation.

9. Results show the crystal structure of the NTF2-like domain of G3BP-1 in complex with nsP3 protein revealing a poly-complex of G3BP-1 dimers interconnected through the FGDF motifs in nsP3. Although in vitro and in vivo binding studies revealed a hierarchical interaction of the two FGDF motifs with G3BP-1, viral growth curves clearly demonstrated that two intact FGDF motifs are required for efficient viral replication.

10. Based on insights from the structures and existing biochemical data, the existence of an evolutionarily conserved ribonucleoprotein (RNP) complex consisting of Caprin-1, FMRP and G3BP1 is proposed.

11. G3BP1 interacts directly with the foot-and-mouth disease virus internal ribosome entry site and negatively regulates translation.

12. The data suggested that JNK-enhanced Tudor-SN phosphorylation promotes the interaction between Tudor-SN and G3BP and facilitates the efficient recruitment of Tudor-SN into stress granules under conditions of sodium arsenite-induced oxidative stress.

13. These data support a role for casein kinase 2 in regulation of protein synthesis by downregulating stress granule formation through G3BP1.

14. G3BP1 is differentially methylated on specific arginine residues by protein arginine methyltransferase (PRMT) 1 and PRMT5 in its RGG domain.

15. Our data define G3BP1 as a novel independent prognostic factor that is correlated with gastric cancer progression.

16. G3BP mediates the condensation of stress granules by shifting between two different states that are controlled by the phosphorylation of S149 and by binding to Caprin1 or USP10.

17. Host G3BP1 captures HIV-1 RNA transcripts and thereby restricts mRNA translation, viral protein production and virus particle formation.

18. Our findings identified a novel function of G3BP1 in the progression of breast cancer via activation of the epithelial-to-mesenchymal transition

19. G3BP1 granules were assembled independently of TIA-1 and had a negative impact on Dengue virus replication.

20. The G3BP1-Caprin1-PKR complex represents a new mode of PKR activation and is important for antiviral activity of G3BP1 and PKR during infection with mengovirus.

Mouse (Murine) GTPase Activating Protein (SH3 Domain) Binding Protein 1 (G3BP1) interaction partners

1. this paper shows that G3BP1 promotes DNA binding and activation of cyclic GMP-AMP synthase

2. the aberrant mutant SOD1-G3BP1 interaction affects stress granule dynamics

3. G3BP is involved in a new functional mechanism to regulate non-coding RNAs including intron-retaining transcripts, and thus have broad implications for neuronal gene regulation, where intron retention is widespread

4. G3bp1 posttranscriptionally regulates miRNA-1 processing in the heart.

5. Our findings identified a novel function of G3BP1 in the progression of breast cancer via activation of the epithelial-to-mesenchymal transition

6. Cytoplasmic granule containing HERMES, NonO, PSF, and G3BP1 is a neuronal RNA-protein granule that is transported in neurites during retinal differentiation.

7. These results show, for the first time, a requirement for G3BP1 in the control of neuronal plasticity and calcium homeostasis

8. Data show that protein kinase R as the principal kinase that mediates eukaryotic initiation factor 2alpha (eIF2alpha) phosphorylation by large RasGAP SH3-binding protein (G3BP)-induced granules.

9. arguments against G3BP1 being a genuine RasGAP-binding partner

10. G3BP1 is a novel Ctnnb1 mRNA binding protein. Methylation of G3BP1 constitutes a molecular switch that regulates Ctnnb1 mRNA in response to Wnt3a.

11. IMP-1 associates with HuD and G3BP-1 proteins in an RNA-dependent manner and binds directly to tau mRNA. We also show an RNA-dependent association between G3BP-1 and HuD proteins

12. the physical interaction between RasGAP and FLN-C facilitates an interaction between G3BP and cdk7 mRNA

13. G3BP is essential for proper embryonic growth and development by mediating the coordinate expression of multiple imprinted growth-regulatory transcripts

Pig (Porcine) GTPase Activating Protein (SH3 Domain) Binding Protein 1 (G3BP1) interaction partners

1. It has been demonstrated a depletion of G3BP1 and TIA-1/TIAR in senescent cells and it was shown that the loss of G3BP1 contributed to impaired stress granules formation.