PMID: 6539785Jul 1, 1984Paper

A membrane cytoskeleton from Dictyostelium discoideum. II. Integral proteins mediate the binding of plasma membranes to F-actin affinity beads

The Journal of Cell Biology
E J LunaH M Ingalls

Abstract

In novel, low-speed sedimentation assays, highly purified, sonicated Dictyostelium discoideum plasma membrane fragments bind to F-actin beads (fluorescein-labeled F-actin on antifluorescein IgG-Sephacryl S-1000 beads). Binding was found to be (a) specific, since beads containing bound fluorescein-labeled ovalbumin or beads without bound fluorescein-labeled protein do not bind membranes, (b) saturable at approximately 0.6 microgram of membrane protein per microgram of bead-bound F-actin, (c) rapid with a t1/2 of 4-20 min, and (d) apparently of reasonable affinity since the off rate is too slow to be measured by present techniques. Using low-speed sedimentation assays, we found that sonicated plasma membrane fragments, after extraction with chaotropes, still bind F-actin beads. Heat-denatured membranes, proteolyzed membranes, and D. discoideum lipid vesicles did not bind F-actin beads. These results indicate that integral membrane proteins are responsible for the binding between sonicated membrane fragments and F-actin on beads. This finding agrees with the previous observation that integral proteins mediate interactions between D. discoideum plasma membranes and F-actin in solution (Luna, E.J., V. M. Fowler, J. Swanson, D. Brant...Continue Reading

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Citations

Jan 1, 1991·Cell Motility and the Cytoskeleton·C P ChiaE J Luna
Nov 15, 1991·Mechanisms of Ageing and Development·C Masters
Dec 24, 2008·Proceedings of the National Academy of Sciences of the United States of America·Charles I Fisher, Scot C Kuo
Jul 1, 1986·Proceedings of the National Academy of Sciences of the United States of America·H M IngallsE J Luna
Jul 1, 1989·Proceedings of the National Academy of Sciences of the United States of America·K G Miller, B M Alberts
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Oct 1, 1985·Journal of Ultrastructure Research·L Rioux, C Gicquaud

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