Key result
Actin filaments are stable under physiological conditions but can be destabilized by a 40 kDa amoeba protein in a Ca2+-dependent manner, while myosin phosphorylation regulates thick-filament formation.
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Actin filaments, assembled from highly purified actin from either skeletal muscle or Dictyostelium amoebae, are very stable under physiological ionic conditions. A small and limited amount of exchange of actin filament subunits for unpolymerized actin or subunits in other filaments has been measured by three techniques: fluorescence energy transfer, incorporation of 35S-labelled actin monomers into unlabelled actin filaments, and exchange of [14C]ATP with filament-bound ADP. A 40 kDa protein purified from amoebae destabilizes these otherwise stable filaments in a Ca2+-dependent manner. Myosin purified from Dictyostelium amoebae is phosphorylated both in the tail region of the heavy chain and in one of the light chains. Phosphorylation appears to regulate myosin thick-filament formation.
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Spudich et al. (1982) studied this question. Actin filaments are stable under physiological conditions but can be destabilized by a 40 kDa amoeba protein in a Ca2+-dependent manner, while myosin phosphorylation regulates thick-filament formation.
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