Mechanism of action of cytochalasin: evidence that it binds to actin filament ends.
To test the idea that cytochalasin retards actin assembly by binding to filament ends, we have designed a new assay for cytochalasin binding in which the number of filament ends can be varied independently of the total actin concentration. Actin is reacted with polylysine-coated polystyrene beads to make filament ends (Brown and Spudich, 1979, J. Cell Biol. 80:499-504) and then reacted with [3H]cytochalasin B. We have found that cytochalasin B binds to beads in the presence of actin, and that the number of cytochalasin B binding sites can be varied as a function of the number of filament ends independent of the total actin concentration by varying the bead concentration.
15 references, click to expand
-
Reductive alkylation of amino groups.Methods Enzymol. 1977;47:469-78 PMID: 927199
-
Biochemical and structural characterization of actin from Dictyostelium discoideum.J Biol Chem. 1978 Dec 25;253(24):9088-96 PMID: 152763
-
Nucleation of polar actin filament assembly by a positively charged surface.J Cell Biol. 1979 Feb;80(2):499-504 PMID: 572366
-
Substoichiometric concentrations of cytochalasin D inhibit actin polymerization. Additional evidence for an F-actin treadmill.J Biol Chem. 1979 Oct 25;254(20):9982-5 PMID: 489616
-
Cytochalasins block actin filament elongation by binding to high affinity sites associated with F-actin.J Biol Chem. 1980 Feb 10;255(3):835-8 PMID: 7356663
-
Spectrin/actin complex isolated from sheep erythrocytes accelerates actin polymerization by simple nucleation. Evidence for oligomeric actin in the erythrocyte cytoskeleton.J Biol Chem. 1980 Feb 25;255(4):1670-6 PMID: 6892570
-
Cytochalasin B and the structure of actin gels.J Mol Biol. 1979 Nov 5;134(3):539-53 PMID: 583431
-
Cytochalasins inhibit nuclei-induced actin polymerization by blocking filament elongation.J Cell Biol. 1980 Feb;84(2):455-60 PMID: 6892916
-
Mechanism of action of cytochalasin B on actin.Cell. 1980 Jun;20(2):329-41 PMID: 6893016
-
ATP-driven steady-state exchange of monomeric and filamentous actin from Dictyostelium discoideum.Proc Natl Acad Sci U S A. 1980 Aug;77(8):4610-3 PMID: 6933508
-
Phagocytosis of latex beads by Acanthamoeba. I. Biochemical properties.Biochemistry. 1967 Feb;6(2):485-97 PMID: 4860149
-
Evidence for biased bidirectional polymerization of actin filaments using heavy meromyosin prepared by an improved method.J Cell Biol. 1975 Oct;67(1):231-7 PMID: 240859
-
Polymerization polarity of actin.J Mechanochem Cell Motil. 1976 Mar;3(3):163-9 PMID: 932564
-
Uni-directional growth of F-actin.J Biochem. 1976 Jan;79(1):159-71 PMID: 780347
-
Head to tail polymerization of actin.J Mol Biol. 1976 Nov;108(1):139-50 PMID: 1003481
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