Effect of caldesmon on the assembly of smooth muscle myosin.

Smooth muscle myosin filaments are much less stable than the skeletal muscle counterpart. Smooth myosin requires higher concentration of Mg2+ than skeletal myosin to form thick filaments and addition of ATP disassembles the dephosphorylated smooth muscle myosin filaments into monomers but not phosphorylated ones. We found that the addition of caldesmon to dephosphorylated myosin induced the formation of the filaments under the conditions where myosin by itself is soluble or disassembled. Although the induced filaments were short at 1 mM Mg2+, they became medium sized and seemed like side polar filaments with prominent 14 nm periodicity at higher Mg2+ conditions (8 mM). In the presence of F-actin, myosin filaments induced by caldesmon were associated along actin filaments to form large structures. The association of actin and myosin filaments was observed only in the presence of caldesmon, suggesting that caldesmon cross-linked actin and myosin filaments. This cross-linking was disrupted by the addition of calmodulin. Caldesmon-induced filament formation of dephosphorylated myosin in the presence of Mg(2+)-ATP may explain the existence of myosin filaments in relaxed smooth muscle fibers. A similar effect of telokin on myosin filament assembly was also examined and is discussed.