UMMS Affiliation
Department of Cell Biology
Publication Date
7-1-1988
Document Type
Article
Subjects
Actins; Cell Membrane; Cross-Linking Reagents; Dictyostelium; Microfilaments; Models, Biological; Polymers
Disciplines
Cell Biology | Life Sciences | Medicine and Health Sciences
Abstract
We have shown previously (Schwartz, M. A., and E. J. Luna. 1986. J. Cell Biol. 102: 2067-2075) that actin binds with positive cooperativity to plasma membranes from Dictyostelium discoideum. Actin is polymerized at the membrane surface even at concentrations well below the critical concentration for polymerization in solution. Low salt buffer that blocks actin polymerization in solution also prevents actin binding to membranes. To further explore the relationship between actin polymerization and binding to membranes, we prepared four chemically modified actins that appear to be incapable of polymerizing in solution. Three of these derivatives also lost their ability to bind to membranes. The fourth derivative (EF actin), in which histidine-40 is labeled with ethoxyformic anhydride, binds to membranes with reduced affinity. Binding curves exhibit positive cooperativity, and cross-linking experiments show that membrane-bound actin is multimeric. Thus, binding and polymerization are tightly coupled, and the ability of these membranes to polymerize actin is dramatically demonstrated. EF actin coassembles weakly with untreated actin in solution, but coassembles well on membranes. Binding by untreated actin and EF actin are mutually competitive, indicating that they bind to the same membrane sites. Hill plots indicate that an actin trimer is the minimum assembly state required for tight binding to membranes. The best explanation for our data is a model in which actin oligomers assemble by binding to clustered membrane sites with successive monomers on one side of the actin filament bound to the membrane. Individual binding affinities are expected to be low, but the overall actin-membrane avidity is high, due to multivalency. Our results imply that extracellular factors that cluster membrane proteins may create sites for the formation of actin nuclei and thus trigger actin polymerization in the cell.
DOI of Published Version
10.1083/jcb.107.1.201
Source
J Cell Biol. 1988 Jul;107(1):201-9. Link to article on publisher's website
Journal/Book/Conference Title
The Journal of cell biology
Related Resources
PubMed ID
3392099
Repository Citation
Schwartz, M. A. and Luna, Elizabeth J., "How actin binds and assembles onto plasma membranes from Dictyostelium discoideum" (1988). Women’s Health Research Faculty Publications. 283.
https://escholarship.umassmed.edu/wfc_pp/283
