•Co-localization was observed between mutant SOD1 (L144F) with G3BP1unlike WT-SOD1 protein in fibroblast cells.•The slight association of mutant SOD1 protein with several other RNA-binding proteins in ALS indicated that these interactions were more specific to the G3BP1 protein.•The RRM domain of G3BP1 and two phenylalanine residues (F380 and F382) are important for desired interactions.•SOD1 mutations and their effects on SG dynamics can be strongly associated with the characteristics and pathogenesis of ALS. This evidence concerns the gene G3BP1 and amyotrophic lateral sclerosis.