Latrunculin A

Latrunculin A is a bioactive 2-thiazolidinone macrolide derived from the red sea sponge Latrunculia magnifica, that sequesters G-actin and prevents F-actin assembly. It binds monomeric actin with 1:1 stoichiometry and can be used to block actin polymerization both in vitro and cells[1,2].

Latrunculin A (1-10 μM) causes tumor cytoskeleton disaggregation in ten minutes[3]. Treatment of cells with latrunculin A at 10 μM overnight strongly inhibits actin synthesis [4].

References：

[1]. Yarmola E G, Somasundaram T, Boring T A, et al. Actin-latrunculin A structure and function. The Journal of Biological Chemisty, 2000, 275(36): 28120-28127.

[2]. Loubéry S, Wilhelm C, Hurbain I, et al. Different microtubule motors move early and late endocytic compartments. Traffic, 2008, 9(4): 492-509.

[3]. Hayot C, Debeir O, Van Ham P, et al. Characterization of the activities of actin-affecting drugs on tumor cell migration. Toxicology and Applied Pharmacology, 2006, 211(1): 30-40.

[4]. Lyubimova A, Bershadsky A D, Ben-Ze'ev A. Autoregulation of actin synthesis requires the 3'-UTR of actin mRNA and protects cells from actin overproduction. Journal of Cellular Biochemistry, 1999, 76(1): 1-12.