Distinct stages in stress granule assembly and disassembly
By Joshua R. Wheeler, T. Matheny, Saumya Jain, Robert G. Abrisch, R. Parker. eLife, 2016
680 citations recorded by the source corpus.
Stress granules are non-membrane bound RNA-protein (RNP) assemblies that form when translation initiation is limited and contain a biphasic structure with stable core structures surrounded by a less concentrated shell. The order of assembly and disassembly of these two structures remains unknown. Time course analysis of granule assembly suggests that core formation is an early event in granule assembly. Stress granule disassembly is also a stepwise process with shell dissipation followed by core clearance. Perturbations that alter liquid-liquid phase separations (LLPS) driven by intrinsically disordered protein regions (IDR) of RNA binding proteins in vitro have the opposite effect on stress granule assembly in vivo. Taken together, these observations argue that stress granules assemble through a multistep process initiated by stable assembly of untranslated mRNPs into core structures, which could provide sufficient high local concentrations to allow for a localized LLPS driven by IDRs on RNA binding proteins. DOI: http://dx.doi.org/10.7554/eLife.18413.001
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/595bd713b346f5d1bda735988dba03e5837a1483
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Citations in the corpus
- Context-Dependent and Disease-Specific Diversity in Protein Interactions within Stress Granules (2018, background): “They also contain a significantly higher proportion of amino acid residues in IDRs and LCDs (Figure 6D) than the background proteome, consistent with LLPS being a driver of SG assembly.”
- Competing protein-RNA interaction networks control multiphase intracellular organization (2020, neutral): “These micron-sized RNA-protein droplets form in mammalian cells upon translational arrest and subsequent polysome disassembly, which releases exposed RNA into the cytoplasm (‘‘RNA influx’’) (Boeynaems et al., 2017; Kedersha et al., 1999, 2002, 2016; Kroschwald et al., 2015; Molliex et al., 2015; Whe”
- Liquid phase condensation in cell physiology and disease (2017, background): “Yeast stress granules also exhibit solid-like features, yet possibly without involving amyloid-like assembly (103), and mammalian stress granules contain solid-like cores, surrounded by a more liquid-like phase (62, 84).”