Key result
Coactosin counteracted the capping activity of cap32/34 and severin domain 1, restoring the time course of actin polymerization close to controls without capping proteins.
Coactosin interferes with the capping of actin filaments by capping proteins, restoring normal actin polymerization kinetics in vitro.
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Hypothesis-generating for actin regulation; leaves open any role in cardiac cytoskeletal function pending in vivo studies.
Coactosin, a 16 kDa protein associated with the actin cytoskeleton from Dictyostelium discoideum, was purified by an improved method, in which other components of the cytoskeleton were removed. The highly purified coactosin had no effect on the time course of actin polymerization, but when added to actin in presence of capping proteins, coactosin counteracted the capping activity of these proteins. The capping proteins cap32/34 and severin domain 1 retarded actin polymerization, on addition of coactosin to samples containing one of these capping proteins the time course of actin polymerization became close to controls without capping proteins.
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Röhrig et al. (1995) studied this question. Coactosin vs. Controls without capping proteins was evaluated on Time course of actin polymerization. Coactosin counteracted the capping activity of cap32/34 and severin domain 1, restoring the time course of actin polymerization close to controls without capping proteins.
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