[2] Use of latrunculin-A, an actin monomer-binding drug
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Actin Assembly Dynamics and Its Regulation in Motile and Morphogenetic Processes
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2008, Biophysical JournalCitation Excerpt :We next examined the effects of another drug, cytochalasin D. Its mode of action on actin organization is different from that of latrunculin A. While latrunculin A binds to actin monomers and blocks their polymerization, resulting in the amount of actin filaments (53,54), cytochalasin D at micromolar concentrations binds to both the barbed and pointed ends of actin filaments and prevents their further polymerization, as well as their interactions with other barbed-end binding proteins (55). While the treatment with 1 μM latrunculin A for 5–20 min (all of the observations were conducted within 20 min after latrunculin addition) strongly affected the molecular motion, the treatment with 1 and 10 μM cytochalasin D for 2–12 min influenced neither the compartment size nor the apparent residency time, under the conditions where the cells did not round up, but the number of stress fibers was decreased and actin clusters were formed (Fig. 9, cyan open bars, Data S1, Fig. S1rows c and d, and Table 2).
Actin-based modeling of a transcriptionally competent nuclear substructure induced by transcription inhibition
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