The actin cytoskeleton is a critical regulator of cytoplasmic architecture and mechanics, essential in a myriad of physiological processes. Here we demonstrate a liquid phase of actin filaments in the presence of the physiological cross-linker, filamin. Filamin condenses short actin filaments into spindle-shaped droplets, or tactoids, with shape dynamics consistent with a continuum model of anisotropic liquids. We find that cross-linker density controls the droplet shape and deformation timescales, consistent with a variable interfacial tension and viscosity. Near the liquid-solid transition, cross-linked actin bundles show behaviors reminiscent of fluid threads, including capillary instabilities and contraction. These data reveal a liquid droplet phase of actin, demixed from the surrounding solution and dominated by interfacial tension. These results suggest a mechanism to control organization, morphology, and dynamics of the actin cytoskeleton.actin | phase separation | liquid crystal | cytoskeleton T he cellular cytoplasm is a hierarchical array of diverse, soft materials assembled from biological molecules that work in concert to support cell physiology (1). The actin cytoskeleton constitutes a spectrum of materials constructed from the semiflexible polymer actin (F-actin) that are crucial in diverse physical processes ranging from cell division and migration to tissue morphogenesis (2, 3). Cross-linking and regulatory proteins assemble actin filaments into bundles and networks with varied composition, mechanics, and physiological function (4). The mechanical properties of actin assemblies regulate force generation and transmission to dynamically control morphogenic processes from the subcellular to tissue length scales (5, 6).A mechanistic understanding of cytoplasmic mechanics is obscured by the rich complexity of in vivo cytoskeletal assemblies (7) and has been investigated via in vitro model systems (8, 9). Vastly different material properties have been accessed through varying filament length, concentration, and cross-linking. For semidilute concentrations of long actin filaments (>1 μm), the mean spacing between actin filaments, or mesh size, is much smaller than the filament length. In this case, cross-linking proteins mechanically constrain actin filaments to result in space-spanning networks that are viscoelastic gels (10). The structure of cross-linked actin networks is kinetically determined, reflecting a metastable state (11, 12) that requires motor-driven stresses for significant shape changes (13). In contrast, highly concentrated solutions of short actin filaments (<1 μm) align due to entropic effects and form equilibrium liquid crystal phases (14). Liquid crystal theory has been introduced as a framework to understand actin cortex mechanics and mitotic spindle shape (5, 15), but the existence of liquid crystal-like phases at physiological conditions is uncertain.Liquid-like phases of proteins and nucleic acids have been found within the cytoplasm and are thought to be important in subcellular...