Myosins constitute a diverse superfamily of actin-based mechanoenzymes
that are involved in many essential cellular motilities. In addition
to conventional muscle myosin II, ten other classes of unconventional
myosins are known. Many unconventional myosins bind multiple calmoduli
n light chains and Ca2+, which can dramatically alter their mechanoche
mical and enzymatic activity. Calmodulin-binding myosins can also be r
egulated by phospholipid binding, phosphorylation of the heavy chain a
nd actin-binding proteins. The molecular details linking unconventiona
l-myosin regulation and function are just beginning to emerge.