G3BP2

Can mediate both protein-protein and protein-RNA interactions via the NTF2 domain and RNA-binding domain RRM; protein-protein and protein-RNA interactions are essential for undergoing liquid-liquid phase separation (LLPS).

The acidic disordered region acts as a negative regulator of phase separation.

The NTF2 domain mediates interaction with CAPRIN1 and USP10 regulators, thereby regulating assembly of stress granules.

Scaffold protein that plays an essential role in cytoplasmic stress granule formation which acts as a platform for antiviral signaling (PubMed:23279204, PubMed:32302570, PubMed:32302571, PubMed:32302572). Plays an essential role in stress granule formation (PubMed:27022092, PubMed:32302570, PubMed:32302571, PubMed:32302572, PubMed:35977029). Stress granules are membraneless compartments that store mRNAs and proteins, such as stalled translation pre-initiation complexes, in response to stress (PubMed:32302570, PubMed:32302571, PubMed:32302572). Promotes formation of stress granules phase-separated membraneless compartment by undergoing liquid-liquid phase separation (LLPS) upon unfolded RNA-binding: functions as a molecular switch that triggers RNA-dependent LLPS in response to a rise in intracellular free RNA concentrations (By similarity).

(Microbial infection) Cleaved by foot-and-mouth disease virus leader protease; this cleavage suppresses the formation of cytoplasmic stress granules.

• Cytoplasm
• Cytoplasm
• Stress granule

KIAA0660, G3BP2, Ras GTPase-activating protein-binding protein 2, G3BP-2, GAP SH3 domain-binding protein 2

• entrezGene:9908
• swissprot:Q9UN86

Proteins

54121Da