Computational modeling and theoretical analysis reveal how disordered linkers determine whether linear multivalent proteins undergo gelation with or without phase separation.

Binding of a multivalent RNA-binding protein to mRNAs that are able to form pervasive RNA–RNA interactions induces formation of mesh-like condensates, whereas binding of mostly structured mRNAs induces sphere-like condensates.

The protein Pat1 functions in the assembly of processing bodies, cellular membraneless organelles, by promoting the liquid–liquid phase separation of the DEAD-box ATPase Dhh1 and RNA.

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.

The current understanding of phase separation is summarized and its emerging roles in cancer are discussed in detail.

A theoretical model explains how protein density and nuclear to cell volume ratio are maintained during cell growth, discusses conditions under which this breaks down, and highlights the importance of metabolites, mainly amino acids such as glutamate, in this homeostasis.

The nucleoplasm surrounding nucleoli in living cells plays a key role in nucleolar dynamics and shape fluctuations in vivo.

Molecules in the condensed phase of biological condensates convert between transiently confined states and mobile states by forming dynamic percolated networks.

Multi-scale simulations reveal a potential, ATP-independent mechanism resulting in the formation of the long-living multi-droplet state by multi-valent, spacer-sticker proteins.

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