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

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

The formation of long-term memory in mice requires an element of RNA granules that localizes messenger RNAs to dendrites.

Cellular stress induces RNA decay that depends on stress granule assembly and is mediated by XRN1, independent of poly(A) tail and 5' cap removal.

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

Expanded repeat RNAs associated with human neurodegenerative diseases can become incorporated into transported granules in neurons, perturbing their function to cause neuritic branching defects.

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.

RNA interference pathways are spatially and temporally organized during Caenorhabditis elegans embryogenesis, with the Argonaute protein NRDE-3 playing distinct roles in regulating genes in different cell types and developmental stages.

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

The RNA-mediated higher order assembly of TDP-43, a protein associated with neurodegenerative diseases, preserves its solubility by reducing the risk of multivalent interactions between low complexity domains.