Dyneins are multisubunit, high molecular weight ATPases that interact with microtubules to generate force by converting the chemical energy of ATP into the mechanical energy of movement. Cytoplasmic or axonemal Dynein heavy, intermediate, light and light-intermediate chains are all components of minus end-directed motors; the complex transports cellular cargos towards the central region of the cell. Axonemal Dynein motors contain one to three non-identical heavy chains and cause a sliding of microtubules in the axonemes of cilia and flagella in a mechanism necessary for cilia to beat and propel the cell. Cytoplasmic Dyneins, such as Dynein IC1, cytosolic and Dynein IC2, cytosolic, comprise an approximately 12 subunit complex of two heavy chains, two intermediate chains to anchor Dynein to its cargo, four smaller intermediate chains and several light chains. This complex performs functions necessary for cell survival, such as organelle transport and centrosome assembly. The carboxy terminus of Dynein is important for microtubule-dependent motility and is highly conserved, while the amino terminal regions are more variable. Several proteins regulate Dynein activity, including dynactin, LIS1 and NudEL (NudE-like).