Cytochalasins inhibit nuclei-induced actin polymerization by blocking filament elongation

Diane Chang Lin, Katherine Dugan Tobin, Martin Grumet, Shin Lin

Research output: Contribution to journalArticle

168 Citations (Scopus)

Abstract

Polylysine was found to induce polymerization of muscle actin in a low ionic strength buffer containing 0.4 mM MgCl2. The rate of induced polymerization was dependent on the amount and on the molecular size of the polylysine added. A similar effect was obtained by adding actin nuclei (containing about 2-4 actin subunits) cross-linked by p-NN′-phenylenebismaleimide to G-actin under the same conditions, suggesting that the effect ofpolylysine is due to promotion of the formation of actin nuclei. Polymerization induced by polylysine and by crosslinked actin nuclei was inhibited by low concentrations (10-8-10-6 M) of cytochalasins. Binding experiments showed that actin filaments, but not actin monomers, contained high-affinity binding sites for [3H]cytochalasin B (one site per 600 actin monomers). The relative affinity of several cytochalasins for these sites (determined by competitive displacement of [3H]dihydrocytochalasin B) was: cytochalasin D > cytochalasin E ≅ dihydrocytochalasin B. The results of this study suggest that cytochalasins inhibit nuclei-induced actin polymerization by binding to highly specific sites at the point of monomer addition, i.e., the elongation site, in actin nuclei and filaments.

Original languageEnglish (US)
Pages (from-to)455-460
Number of pages6
JournalJournal of Cell Biology
Volume84
Issue number2
DOIs
StatePublished - Feb 1 1980

Fingerprint

Cytochalasins
Polymerization
Actins
Polylysine
Actin Cytoskeleton
Cytochalasin D
Cytochalasin B
Magnesium Chloride
Osmolar Concentration
Buffers
Binding Sites

All Science Journal Classification (ASJC) codes

  • Cell Biology

Keywords

  • Actin filaments
  • Actin polymerization
  • Cell motility
  • Cytochalasins
  • Cytoskeleton

Cite this

Lin, Diane Chang ; Tobin, Katherine Dugan ; Grumet, Martin ; Lin, Shin. / Cytochalasins inhibit nuclei-induced actin polymerization by blocking filament elongation. In: Journal of Cell Biology. 1980 ; Vol. 84, No. 2. pp. 455-460.
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Cytochalasins inhibit nuclei-induced actin polymerization by blocking filament elongation. / Lin, Diane Chang; Tobin, Katherine Dugan; Grumet, Martin; Lin, Shin.

In: Journal of Cell Biology, Vol. 84, No. 2, 01.02.1980, p. 455-460.

Research output: Contribution to journalArticle

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T1 - Cytochalasins inhibit nuclei-induced actin polymerization by blocking filament elongation

AU - Lin, Diane Chang

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N2 - Polylysine was found to induce polymerization of muscle actin in a low ionic strength buffer containing 0.4 mM MgCl2. The rate of induced polymerization was dependent on the amount and on the molecular size of the polylysine added. A similar effect was obtained by adding actin nuclei (containing about 2-4 actin subunits) cross-linked by p-NN′-phenylenebismaleimide to G-actin under the same conditions, suggesting that the effect ofpolylysine is due to promotion of the formation of actin nuclei. Polymerization induced by polylysine and by crosslinked actin nuclei was inhibited by low concentrations (10-8-10-6 M) of cytochalasins. Binding experiments showed that actin filaments, but not actin monomers, contained high-affinity binding sites for [3H]cytochalasin B (one site per 600 actin monomers). The relative affinity of several cytochalasins for these sites (determined by competitive displacement of [3H]dihydrocytochalasin B) was: cytochalasin D > cytochalasin E ≅ dihydrocytochalasin B. The results of this study suggest that cytochalasins inhibit nuclei-induced actin polymerization by binding to highly specific sites at the point of monomer addition, i.e., the elongation site, in actin nuclei and filaments.

AB - Polylysine was found to induce polymerization of muscle actin in a low ionic strength buffer containing 0.4 mM MgCl2. The rate of induced polymerization was dependent on the amount and on the molecular size of the polylysine added. A similar effect was obtained by adding actin nuclei (containing about 2-4 actin subunits) cross-linked by p-NN′-phenylenebismaleimide to G-actin under the same conditions, suggesting that the effect ofpolylysine is due to promotion of the formation of actin nuclei. Polymerization induced by polylysine and by crosslinked actin nuclei was inhibited by low concentrations (10-8-10-6 M) of cytochalasins. Binding experiments showed that actin filaments, but not actin monomers, contained high-affinity binding sites for [3H]cytochalasin B (one site per 600 actin monomers). The relative affinity of several cytochalasins for these sites (determined by competitive displacement of [3H]dihydrocytochalasin B) was: cytochalasin D > cytochalasin E ≅ dihydrocytochalasin B. The results of this study suggest that cytochalasins inhibit nuclei-induced actin polymerization by binding to highly specific sites at the point of monomer addition, i.e., the elongation site, in actin nuclei and filaments.

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