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Spontaneous osmoregulation in giant phospholipid vesicles, which is characterized by oscillations in vesicle size and membrane tension, couples to the compositional degrees of freedom at the membrane surface to produce oscillations in domain texture and induce isothermal phase change.

Phase separation of two-component multivalent systems is suppressed at rational polymer stoichiometries, suggesting possible cellular strategies for regulating the formation and function of biomolecular condensates.

Clustering the B cell receptor generates a membrane domain analogous to the liquid-ordered phase, localizing proteins involved in early receptor activation.

A general mechanism for how powerful forces of assembly and protein mobility can emerge from phase transitions is established.

B-cell receptors form ordered clusters to recruit kinases and exclude phosphatases.

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

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.

An outer membrane vesicle pulse-chase assay demonstrates that the Acinetobacter baumannii Mla system is a retrograde lipid transporter.

Transient DNA interactions by DNA-binding proteins are utilized by herpes simple virus as an alternative route to generate membraneless compartments in the nucleus without invoking phase separation.

OptoGranules reveal the function of G3BP1 as a stress granule scaffold and demonstrate that protracted stress granule assembly is sufficient to drive neurodegeneration and the evolution of ALS-FTD pathology.