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

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.

Intersectin counterparts in yeast recruit WASP and WIP to endocytic sites to establish a robust multivalent SH3 domain-PRM interaction network which gives actin assembly onset a switch-like behavior in vivo.

De novo protein nanoparticles were designed from scratch to present viral glycoprotein antigens, providing a systematic way to study the influence of antigen presentation geometry on immune response.

Binding of multiple LC8 copies to the intrinsically disordered region of the transcription factor ASCIZ exemplifies a new and potentially widespread molecular mechanism for negative feedback regulation.

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.

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.

Computer simulations of model proteins with sticker-and-spacer architectures shed light on the formation of biomolecular condensates in cells.

A membrane-associated, supramolecular protein complex with dynamically changing components, the central supramolecular activation cluster, regulates the generation of the T cell effector cytokine IL-2 depending on its composition.

An activator of branching nucleation by Arp2/3 complex directly synergizes with an activator of linear filament nucleation to initiate assembly of actin networks that drive endocytosis.