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Significance Muscle myosins polymerize into thick filaments that drive muscle contraction by interaction with actin thin filaments. The details of muscle myosin polymerization into thick filaments are not known. Current hypotheses are that elongated myosin monomers form antiparallel dimers that polymerize into filaments. However, we find polymerization in vitro of skeletal, cardiac, and smooth muscle myosins involves formation of monomers with folded tails, tail-folded dimers, and tail-folded tetramers. These observations should stimulate studies of the pathway of formation of muscle myosins in vitro and in vivo including the possible roles of the multiple myosin-associated proteins on in vivo polymerization.

Muscle myosins form folded monomers, dimers, and tetramers during filament polymerization in vitro