The intrinsically-disordered protein MEG-3 recruits mRNAs to P granules by forming gel-like condensates with ribosome-depleted mRNAs.

P granule assembly depends in part on protein-protein interactions that drive condensation independent of RNA.

A competition for RNA drives the localized assembly of RNA granules in the C. elegans embryo.

The MEG (maternal-effect germline defective) proteins, MEG-1, 2, 3 and 4, regulate RNA granule dynamics in vivo.

Two novel LOTUS-domain proteins are core germ granule components that directly recruit Caenorhabditis elegans Vasa, regulate germ granule size and localization, and provide an organizational framework for ribonucleoprotein complexes.

A comparison in yeast and human cells reveals a remarkable variability in the properties of RNP granules and highlights a key role for protein disaggregation machines in regulating RNP granule assembly.

A proximity labeling approach defines germ granule proteome in Caenorhabditis elegans, and identifies LOTUS domain proteins as key regulators of germ granule assembly.

Liquid-liquid phase separation of a rhabovirus phosphoprotein initiates viral factory formation of barley yellow striate mosaic virus, a plant negative-sense RNA virus, and host casein kinase 1-mediated phosphorylation inhibits phase separation and virus infection.

SIMR-1 acts downstream of the piRNA pathway to promote siRNA amplification by the Mutator complex and localizes to perinuclear foci distinct from Mutator foci, P granules and Z granules.

A newly discovered substrate of Pak1 kinase reveals novel mechanisms that control cell shape through regulated assembly of ribonucleoprotein granules.