The myosin regulatory and essential light chains in skeletal muscle do not play a role as significant as in scallop or smooth muscle, however, there are some data suggesting that the skeletal myosin light chains and their N-terminal parts may have a modulatory function in the interaction of actin with myosin heads. In this paper four conformational states of the myosin head with respect to the regulatory light chain bound cation (magnesium or calcium) and phosphorylation are proposed. Communication between regulatory and essential light chains and putative binding of the N-terminus of A1 essential light chain to actin is discussed.
