English: Schematic representation of stress granule (SG) dynamics. Upon stress condition, SGs assemble; RNA and proteins accumulate in these granules until the stress desists. After removal of the stress condition, SGs disassemble, protein synthesis is reactivated after the translation inhibition induced by the stress, and RBPs can either go back to the nucleus or remain in the cytoplasm, where they carry out their normal functions. Misfolded proteins can accumulate in SGs, thus altering their physical properties. To prevent the accumulation of misfolded proteins, therapeutic strategies, such as chaperones, potentiated chaperones, protein kinases (e.g., DYRK3), nuclear import receptors, and ASOs, can be engineered to induce SG disassembly. If the disassembly does not occur, SGs become aberrant and can promote the pathogenesis of neurodegenerative disorders. Finally, aberrant SGs can undergo disassembly by chaperones, potentiated chaperones, or kinases, and, if not repaired, they undergo degradation by autophagy.^[1]