A combination of imaging experiments and computer simulations on a model lipid membrane integrate the 'picket fence' and 'raft' models, and suggest that the interplay between actin binding, lipid phase separation and curvature compartmentalize the membrane.

A new and general mechanism describes the organization of membrane proteins and their cytoplasmic ligands into micrometer-scale clusters, based on polymerization and concomitant phase separation of multivalent proteins.

The damage of the bacterial cell envelope is found to be only a secondary effect of the antimicrobial activity of lactoferricin derivatives.

Biochemical and cell biological data suggest a model of nascent integrin adhesion complex formation based on synergistic phase separation of pathways surrounding the focal adhesion kinase (FAK) and the adaptor protein p130Cas.

Two competing descriptions of membrane-less sub-compartments, liquid droplets and polymer binding aggregates, can be cast into a common theoretical framework and tested through single-particle tracking experiments.

Biochemical studies and molecular dynamics simulations indicate that dephosphroylation of F-BAR protein Cdc15 promotes cytokinesis ring assembly in yeast via conformation change of intrinsically disorder regions and condensate formation.

Nucleolar protein localization involves the phase separation within the nucleolar matrix via three types of multivalent features: acidic tracts, nucleic acid binding domains and arginine-rich low complexity sequences.

Protein phase separation provides an explanation for the compositional flexibility of endocytic initiation and the role of multivalent disordered scaffolds in endocytosis.

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

EphA2 receptor clustering enhances signaling transductions by increasing receptor phosphorylation and binding dwell time of downstream molecules in living cells.