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Inhibition of actin polymerization by latrunculin A
Author(s) -
Coué Martine,
Brenner Stephen L.,
Spector Ilan,
Korn Edward D.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)81513-2
Subject(s) - in vitro , actin , biophysics , microfilament , marine toxin , sponge , microbiology and biotechnology , chemistry , biology , polymerization , toxin , biochemistry , cytoskeleton , cell , botany , organic chemistry , polymer
Latrunculin A, a toxin purified from the red sea sponge Latrunculia magnifica , was found previously to induce striking reversible changes in the morphology of mammalian cells in culture and to disrupt the organization of their microfilaments. We now provide evidence that latrunculin A affects the polymerization of pureactin in vitro in a manner consistent with the formation of a 1:1 molar complex between latrunculin A and G‐actin. The equilibrium dissociation constant ( K d ) for the reaction in vitro is about 0.2 μM whereas the effects of the drug on cultured cells are detectable at concentrations in the medium of 0.1–1 μM.