Actin polymerization induces a shape change in actin-containing vesicles

J. D. Cortese, B. Schwab, C. Frieden, E. L. Elson

Research output: Contribution to journalArticle

105 Scopus citations

Abstract

We have encapsulated actin filaments in the presence and absence of various actin-binding proteins into lipid vesicles. These vesicles are approximately the same size as animal cells and can be characterized by the same optical microscopic and mechanical techniques used to study cells. We demonstrate that the initially spherical vesicles can be forced into asymmetric, irregular shapes by polymerization of the actin that they contain. Deformation of the vesicles requires that the actin filaments be on average at least ~ 0.5 μm long as shown by the effects of gelsolin, an actin filament-nucleating protein. Filamin, a filament-crosslinking protein, caused the surfaces of the vesicles to have a smoother appearance. Heterogeneous distribution of actin filaments within the vesicles is caused by interfilament interactions and modulated by gelsolin and filamin. The vesicles provide a model system to study control of cell shape and cytoskeletal organization, membrane-cytoskeleton interactions, and cytomechanics.

Original languageEnglish
Pages (from-to)5773-5777
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume86
Issue number15
DOIs
StatePublished - Jan 1 1989

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