Protein motors are chemo-mechanical enzymes that can naturally generate force and move cargo or as individual molecules along tracks of protein polymers (actin filaments or microtubules), using chemical energy from adenosinetriphosphate (ATP) hydrolysis. In order to harness these protein motors to power nanometer-scale devices, we have investigated effective and non-destructive methods for immobilizing them and/or their protein filament tracks on surfaces and to steer the output of these motors, i.e. force and movement, into defined directions. We succeeded in aligning protein motors (myosin and its proteolytic fragments) on microscopic polytetrafluoroethylene (PTFE) ridges deposited on surfaces and showed that movement of actin filaments was then restricted to these PTFE tracks [1,2]. We extended this technique and found polymethylmethacrylate (PMMA) also to be useful for immobilizing myosin molecules while retaining their ability to move actin [3]. However, two major problems need to be solved before these methods are applicable to microactuators. First, the number of actin filaments on the tracks gradually decreased over time owing to their running off the ends of tracks. Secondly, movement of the actin filaments occurred in both directions along the tracks, requiring a way to rectify their bidirectional motion into unidirectional movement. We succeeded in restricting kinesin-driven movement of microtubules along micrometer-scale grooves lithographically fabricated on glass surfaces and unidirectional movement was accomplished simply by adding arrowhead patterns on the tracks [4]. Applications of motor proteins in nanometric fine-movement microactuators are now stepping closer to reality.