Ras GTPase-activating protein-binding protein 1 (G3BP1) mRNA (G3BP1 mRNA)

Ras GTPase-activating protein-binding protein 1 (G3BP1) mRNA encodes a multifunctional RNA-binding protein that serves as the primary nucleator for the assembly of stress granules (SGs) (PubMed: 31064744). Stress granules are membrane-less organelles that sequester mRNAs and proteins during cellular stress to regulate protein synthesis and cell survival (UniProt: Q13283). In many cancers, G3BP1 is upregulated and promotes tumor cell proliferation, invasion, and resistance to apoptosis by stabilizing oncogenic mRNAs (PubMed: 32814841). Furthermore, G3BP1 is a critical host factor for various viruses, including SARS-CoV-2, which utilize it to facilitate viral genome replication or to suppress host antiviral signaling pathways like the cGAS-STING pathway (PubMed: 33053439). Targeting G3BP1 mRNA with nucleic acid-based therapeutics, such as antisense oligonucleotides (ASOs) or small interfering RNAs (siRNAs), provides a strategy to deplete G3BP1 protein levels, thereby inhibiting SG formation and disrupting the survival mechanisms of cancer cells and viruses (PubMed: 34206035). This approach is particularly relevant in overcoming chemoresistance and treating viral infections where G3BP1 is a mandatory co-factor. Research is also exploring the role of G3BP1 in neurodegenerative diseases, where aberrant stress granule formation is a hallmark of pathology (PubMed: 31064744).

Other names

G3BP-1 mRNAGAP SH3 domain-binding protein 1 mRNARasGAP-associated endoribonuclease mRNA

Degradation of target mRNA via RNase H-mediated cleavage or RNA interference (RNAi) to reduce G3BP1 protein expression.