Microtubule (MT) and kinesin are rail and motor proteins that are involved in various moving events of eukaryotic cells in natural systems. In vitro, the sliding motion of microtubules (rail) can be reproduced on a kinesin (motor protein)-coated surface coupled with adenosine triphosphate (ATP) hydrolysis, which is called a "motility assay". Based on this technique, a method was recently established to form MT assemblies by an active self-organization (AcSA) process, in which MTs are crosslinked during a sliding motion on a kinesin-coated surface. Streptavidin (ST) was employed as glue to crosslink biotin-labeled MTs. Various shapes, sizes, and motilities were formed with the AcSA MT assemblies, depending on the initial conditions. In this paper, we briefly review our recent work on the formation of MT assemblies on a kinesin-coated surface.pg. 2