Latrunculin A Accelerates Actin Filament Depolymerization in Addition to Sequestering Actin Monomers.

ABSTRACT: Latrunculin A (LatA), a toxin from the red sea sponge Latrunculia magnifica, is the most widely used reagent to depolymerize actin filaments in experiments on live cells. LatA binds actin monomers and sequesters them from polymerization [1, 2]. Low concentrations of LatA result in rapid (tens of seconds) disassembly of actin filaments in animal [3] and yeast cells [2]. Depolymerization is usually assumed to result from sequestration of actin monomers. Our observations of single-muscle actin filaments by TIRF microscopy showed that LatA bound ATP-actin monomers with a higher affinity (K_d = 0.1 μM) than ADP-P_i-actin (K_d = 0.4 μM) or ADP-actin (K_d = 4.7 μM). LatA also slowly severed filaments and increased the depolymerization rate at both ends of f

SUBMITTER: Fujiwara I 

PROVIDER: S-EPMC6179359 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature