Latrunculin
The latrunculins are a family of natural products and toxins produced by certain sponges, including genus Latrunculia and Negombata, whence the name is derived. It binds actin monomers near the nucleotide binding cleft with 1:1 stoichiometry and prevents them from polymerizing. Administered in vivo, this effect results in disruption of the actin filaments of the cytoskeleton, and allows visualization of the corresponding changes made to the cellular processes. This property is similar to that of cytochalasin, but has a narrow effective concentration range.[1] Latrunculin has been used to great effect in the discovery of cadherin distribution regulation. Latrunculin A, a type of the toxin, was found to be able to make reversible morphological changes to mammalian cells by disrupting the actin network.[2]
References
- ^ Braet, F. (1996). Microfilament-disrupting agent latrunculin A induces and increased number of fenestrae in rat liver sinusoidal endothelial cells: Comparison with cytochalasin B. Hepatology, 24(3), 627-635. doi:10.1053/jhep.1996.v24.pm0008781335
- ^ Coué, M., Brenner, S. L., Spector, I., & Korn, E. D. (1987). Inhibition of actin polymerization by latrunculin A. FEBS Letters, 213(2), 316-318. doi:10.1016/0014-5793(87)81513-2
- Yarmola, E.G., Somasundaram, T., Boring, T.A., Spector, I., Bubb, M.R. (2000). "Actin-Latrunculin A Structure and Function". Journal of Biological Chemistry. 275 (36): 28120–28127. doi:10.1074/jbc.M004253200. PMID 10859320.
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