Regulation and expression of metazoan unconventional myosins

Unconventional myosins are molecular motors that convert adenosine triphosphate (ATP) hydrolysis into movement along actin filaments. On the basis of primary structure analysis, these myosins are represented by at least 15 distinct classes (classes 1 and 3-16), each of which is presumed to play a specific cellular role. However, in contrast to the conventional myosins-2, which drive muscle contraction and cytokinesis and have been studied intensively for many years in both uni- and multicellular organisms, unconventional myosins have only been subject to analysis in metazoan systems for a short time. Here we critically review what is known about unconventional myosin regulation, function, and expression. Several points emerge from this analysis. First, in spite of the high relative conservation of motor domains among the myosin classes, significant differences are found in biochemical and enzymatic properties of these motor domains. Second, the idea that characteristic distributions of unconventional myosins are solely dependent on the myosin tail domain is almost certainly an oversimplification. Third, the notion that most unconventional myosins function as transport motors for membranous organelles is challenged by recent data. Finally, we present a scheme that clarifies relationships between various modes of myosin regulation.