Abstract
To study the morphogenesis of cells caused by the organization of their internal cytoskeletal network, we characterized the transformation of liposomes encapsulating actin and its crosslinking proteins, or tubulin and microtubule associated proteins (MAPs), using high-intensity dark-field microscopy. With increasing temperature, the encapsulated G-action polymerized into actin filaments and formed bundles or gels, depending on the type of actin-crosslinking protein that was co-encapsulated, causing various morphological changes of liposomes. When tubulin was polymerized with MAPs in liposomes, liposomes were transformed into a "bipolar" shape. This shape was stabilized only when MAPs were co-encapsulated.
