Application of stress granule core element G3BP1 in various diseases: A review

Ras-GTPase-activating protein-binding protein 1 (G3BP1) is a core component and crucial regulatory switch in stress granules (SGs). When the concentration of free RNA within cells increases, it can trigger RNA-dependent liquid-liquid phase separation (LLPS) with G3BP1 as the core, thereby forming SGs that affect cell survival or death. In addition, G3BP1 interacts with various host proteins to regulate the expression of SGs. As a multifunctional binding protein, G3BP1 has diverse biological functions, influencing cell proliferation, differentiation, apoptosis, and RNA metabolism and serving as a crucial regulator in signaling pathways such as Rac1-PAK1, TSC-mTORC1, NF-kappa B, and STAT3. Therefore, it plays a significant role in the regulation of neurodegenerative diseases, myocardial hypertrophy, and congenital immunity, and is involved in the proliferation, invasion, and metastasis of cancer cells. G3BP1 is an important antiviral factor that interacts with viral proteins, and regulates SG assembly to exert antiviral effects. This article focuses on the recent discoveries and progress of G3BP1 in biology, including its structure and function, regulation of SG formation and dissolution, and its relationships with non-neoplastic diseases, tumors, and viruses.