Cells are biochemically and morphologically polarized, which allows them to produce different cell shapes for various functions. Remarkably, some polarity protein complexes are asymmetrically recruited and concentrated on limited membrane regions, which is essential for the establishment and maintenance of diverse cell polarity. Though the components and mutual interactions within these protein complexes have been extensively investigated, how these proteins autonomously concentrate at local membranes and whether they have the same organization mechanism in the condensed assembly as that in aqueous solution remain elusive. A number of recent studies suggest that these highly concentrated polarity protein assemblies are membraneless biomolecular condensates which form through liquid-liquid phase separation (LLPS) of specific proteins. In this perspective, we summarize the LLPS-driven condensed protein assemblies found in asymmetric cell division, epithelial cell polarity, and neuronal synapse formation and function. These findings suggest that LLPS may be a general strategy for cells to achieve local condensation of specific proteins, thus establishing cell polarity.