High efficiency, homology-directed genome editing in Caenorhabditis elegans using CRISPR–Cas9 ribonucleoprotein complexes. Organization and function of non-dynamic biomolecular condensates. Mapping local and global liquid phase behavior in living cells using photo-oligomerizable seeds. elegans: a genetic model for the study of RNA–protein condensates. Polar positioning of phase-separated liquid compartments in cells regulated by an mRNA competition mechanism. Toxic PR poly-dipeptides encoded by the C9orf72 repeat expansion target LC domain polymers. Biomolecular condensates: organizers of cellular biochemistry. Coordinate activation of maternal protein degradation during the egg-to-embryo transition in C. Perinuclear P granules are the principal sites of mRNA export in adult C. Regulation of RNA granule dynamics by phosphorylation of serine-rich, intrinsically disordered proteins in C. Spatial patterning of P granules by RNA-induced phase separation of the intrinsically disordered protein MEG-3. The disordered P granule protein LAF-1 drives phase separation into droplets with tunable viscosity and dynamics. DEPS-1 promotes P-granule assembly and RNA interference in C. Genetic analysis of the Caenorhabditis elegans GLH family of P-granule proteins. The PGL family proteins associate with germ granules and function redundantly in Caenorhabditis elegans germline development. PGL proteins self associate and bind RNPs to mediate germ granule assembly in C. Germline P granules are liquid droplets that localize by controlled dissolution/condensation. Distinct stages in stress granule assembly and disassembly. ATPase-modulated stress granules contain a diverse proteome and substructure. Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization. Formation and maturation of phase-separated liquid droplets by RNA-binding proteins. Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels. Cell-free formation of RNA granules: bound RNAs identify features and components of cellular assemblies. Liquid phase condensation in cell physiology and disease. Protein phase separation: a new phase in cell biology. ![]() Liquid–liquid phase separation in biology. Our findings suggest that condensation of RNA granules can be regulated spatially by gel-like polymers that stimulate LLPS locally in the cytoplasm. ![]() Co-assembly of gel phases and liquid phases confers local stability and long-range dynamics, both of which contribute to localized assembly of P granules. The second phase is formed by gel-like assemblies of the disordered protein MEG-3 that associate with liquid PGL-3 droplets in the embryo posterior. We find that the PGL-3 phase is intrinsically labile and requires a second phase for stabilization in embryos. Theoretical studies have suggested that spontaneous LLPS of the RNA-binding protein PGL-3 with RNA drives the assembly of P granules. P granules are RNA granules that form in the posterior of Caenorhabditis elegans embryos. The mechanisms that localize liquid phases in cells, however, are not fully understood. RNA granules are subcellular compartments that are proposed to form by liquid–liquid phase separation (LLPS), a thermodynamic process that partitions molecules between dilute liquid phases and condensed liquid phases.
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