Myosin is a highly conserved, ubiquitously expressed protein that interacts with Actin to generate the force for cellular movements. Conventional myosins are hexameric proteins consisting of two heavy chain subunits, a pair of non-phosphorylatable light chain subunits and a pair of phosphorylatable light chain subunits. Three general classes of myosin have been cloned: smooth muscle myosins, striated muscle myosins and non-muscle myosins. Contractile activity in smooth muscle is regulated by the calcium/calmodulin-dependent phosphorylation of myosin light chain by myosin light chain kinase. Myosin heavy chains are encoded by the MYH gene family and have Actin-activated ATPase activity which generates the motor function of myosin. Myosin heavy chains, which were initially isolated from a human fetal skeletal muscle, are the major determinant in the speed of contraction of skeletal muscle. Various isoforms of myosin heavy chain are differentially expressed depending on the functional activity of the muscle.
