Force generation by molecular motors drives biological processes such as asymmetric cell division and cell migration. Microtubule gliding assays in which surface-immobilized motor proteins drive microtubule propulsion are widely used to study basic motor properties as well as the collective behavior of active self-organized systems. Additionally, these assays can be employed for nanotechnological applications such as analyte detection, biocomputation, and mechanical sensing. While such assays allow tight control over the experimental conditions, spatiotemporal control of force generation has remained underdeveloped. Here we use light-inducible protein-protein interactions to recruit molecular motors to the surface to control microtubule gliding activity in vitro. We show that using these light-inducible interactions, proteins can be recruited to the surface in patterns, reaching a â5-fold enrichment within 6 s upon illumination. Subsequently, proteins are released with a half-life of 13 s when the illumination is stopped. We furthermore demonstrate that light-controlled kinesin recruitment results in reversible activation of microtubule gliding along the surface, enabling efficient control over local microtubule motility. Our approach to locally control force generation offers a way to study the effects of nonuniform pulling forces on different microtubule arrays and also provides novel strategies for local control in nanotechnological applications.
- Motor proteins
- Optical control