To study the morphogenesis of cells caused by the organization of their int
ernal cytoskeletal network, we characterized the transformation of liposome
s encapsulating actin and its crosslinking proteins, fascin, alpha-actinin,
or filamin, using real-time high-intensity dark-field microscopy. With inc
reasing temperature, the encapsulated G-actin polymerized into actin filame
nts and formed bundles or gels, depending on the type of actin-crosslinking
protein that was co-encapsulated, causing various morphological changes of
liposomes. The differences in morphology among transformed liposomes indic
ate that actin-crosslinking proteins determine liposome shape by organizing
their specific actin networks. Morphological analysis reveals that the cro
sslinking manner, i.e. distance and angular flexibility between adjacent cr
osslinked actin filaments, is essential for the morphogenesis rather than t
heir binding affinity and stoichiometry to actin filaments. (C) 1999 Academ
ic Press.