Protein involved in various processes, such as stress granule formation and innate immunity (  ). Plays an essential role in stress granule formation (     ). Stress granules are membraneless compartments that store mRNAs and proteins, such as stalled translation pre-initiation complexes, in response to stress (    ). 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 (  , ). Also acts as an ATP- and magnesium-dependent helicase: unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency . Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA . Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends . Plays an essential role in innate immunity by promoting CGAS and RIGI activity (, ). Participates in the DNA-triggered cGAS/STING pathway by promoting the DNA binding and activation of CGAS . Triggers the condensation of cGAS, a process probably linked to the formation of membrane-less organelles . Enhances also RIGI-induced type I interferon production probably by helping RIGI at sensing pathogenic RNA . May also act as a phosphorylation-dependent sequence-specific endoribonuclease in vitro: Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR .
Subcellular locations: Cytoplasm, Cytosol, Perikaryon, Cytoplasm, Stress granule, Nucleus
Cytoplasmic in proliferating cells . Cytosolic and partially nuclear in resting cells . Recruited to stress granules in response to arsenite treatment (, ). The unphosphorylated form is recruited to stress granules . HRAS signaling contributes to this process by regulating G3BP dephosphorylation .
Ubiquitous.