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G3BP1 Is a Tunable Switch that Triggers Phase Separation to Assemble Stress Granules. | LitMetric

AI Article Synopsis

  • The assembly of stress granules (SGs), a type of ribonucleoprotein granule, occurs through a process called liquid-liquid phase separation (LLPS), driven by uneven interactions in a protein-RNA network.
  • G3BP1 is identified as a crucial component that acts as a molecular switch, promoting LLPS when free RNA levels increase inside cells.
  • The regulation of SG assembly involves the intrinsic disordered regions of G3BP1 and their phosphorylation, along with the influence of other factors that can either enhance or inhibit the core SG formation network.

Article Abstract

The mechanisms underlying ribonucleoprotein (RNP) granule assembly, including the basis for establishing and maintaining RNP granules with distinct composition, are unknown. One prominent type of RNP granule is the stress granule (SG), a dynamic and reversible cytoplasmic assembly formed in eukaryotic cells in response to stress. Here, we show that SGs assemble through liquid-liquid phase separation (LLPS) arising from interactions distributed unevenly across a core protein-RNA interaction network. The central node of this network is G3BP1, which functions as a molecular switch that triggers RNA-dependent LLPS in response to a rise in intracellular free RNA concentrations. Moreover, we show that interplay between three distinct intrinsically disordered regions (IDRs) in G3BP1 regulates its intrinsic propensity for LLPS, and this is fine-tuned by phosphorylation within the IDRs. Further regulation of SG assembly arises through positive or negative cooperativity by extrinsic G3BP1-binding factors that strengthen or weaken, respectively, the core SG network.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7448383PMC
http://dx.doi.org/10.1016/j.cell.2020.03.046DOI Listing

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