During mitosis and meiosis, the bipolar spindle facilitates chromosome segregation through microtubule sliding as well as microtubule growth and shrinkage. Kinesin-14, one of the motors involved, causes spindle collapse in the absence of kinesin-5 (Refs 2, 3), participates in spindle assembly and modulates spindle length. However, the molecular mechanisms underlying these activities are not known. Here, we report that Drosophila melanogaster kinesin-14 (Ncd) alone causes sliding of anti-parallel microtubules but locks together (that is, statically crosslinks) those that are parallel. Using single molecule imaging we show that Ncd diffuses along microtubules in a tail-dependent manner and switches its orientation between sliding microtubules. Our results show that kinesin-14 causes sliding and expansion of an anti-parallel microtubule array by dynamic interactions through the motor domain on the one side and the tail domain on the other. This mechanism accounts for the roles of kinesin-14 in spindle organization.

Inside cells, motor proteins perform a variety of complex tasks including the transport of vesicles and the separation of chromosomes. We demonstrate a novel use of such biological machines for the mechanical manipulation of nanostructures in a cell-free environment. Specifically, we show that purified kinesin motors in combination with chemically modified microtubules can transport and stretch individual λ-phage DNA molecules across a surface. This technique, in contrast to existing ones, enables the parallel yet individual manipulation of many molecules and may offer an efficient mechanism for assembling multidimensional DNA structures.

The synthesis of Si nanowires in nanoporous anodic alumina membranes was demonstrated using a combination of Au electrodeposition and vapor-liquid-solid growth at 500°C using SiH 4 as the Si source. The average diameter of the nanowires was 200Ϯ54 nm which was close to the pore size distribution of the membranes. High-resolution transmission electron microscopy revealed that the nanowires consist of a crystalline Si core, oriented in the ͗100͘ or ͗211͘ growth direction, with a thin (Ͻ3 nm) native oxide coating. In this process, Au terminates both ends of the growing wires, resulting in the formation of Au-Si-Au nanowires.

We report on the generation of nanometer-wide, non-topographical patterns of proteins on planar surfaces. In particular, we used the regular lattice of reconstituted microtubules as template structures to specifically bind and transfer kinesin-1 and nonclaret disjunctional motor proteins. The generated tracks, which comprise dense and structurally oriented arrays of functional motor proteins, proved to be highly efficient for the guiding of microtubule transporters.

Over the last 25 years, extensive progress has been made in developing a range of nanotechnological applications where cytoskeletal filaments and molecular motors are key elements. This includes novel, highly miniaturized lab on a chip systems for biosensing, nanoseparation etc but also new materials and parallel computation devices for solving otherwise intractable mathematical problems. For such approaches, both actin-based and microtubule-based cytoskeletal systems have been used. However, in accordance with their different cellular functions, actin filaments and microtubules have different properties and interaction kinetics with molecular motors. Therefore, the two systems obviously exhibit different advantages and encounter different challenges when exploited for applications. Specifically, the achievable filament velocities, the capability to guide filaments along nanopatterned tracks and the capability to attach and transport cargo differ between actin- and microtubule-based systems. Our aim here is to systematically elucidate these differences to facilitate design of new devices and optimize future developments. We first review the cellular functions and the fundamental physical and biochemical properties of actin filaments and microtubules. In this context we also consider their interaction with molecular motors and other regulatory proteins that are of relevance for applications. We then relate these properties to the advantages and challenges associated with the use of each of the motor-filament systems for different tasks. Finally, fundamental properties are considered in relation to some of the most interesting future development paths e.g. in biosensing and biocomputation.

Molecular motors, highly efficient biological nanomachines, hold the potential to be employed for a wide range of nanotechnological applications. Toward this end, kinesin, dynein, or myosin motor proteins are commonly surface-immobilized within engineered environments in order to transport cargo attached to cytoskeletal filaments. Being able to flexibly control the direction of filament motion, and in particular on planar, non-topographical surfaces, has, however, remained challenging. Here, we demonstrate the applicability of a UV-laser-based ablation technique to programmably generate highly localized patterns of functional kinesin-1 motors with different shapes and sizes on PLL-g-PEG-coated polystyrene surfaces. Straight and curved motor tracks with widths of less than 500 nm could be generated in a highly reproducible manner and proved to reliably guide gliding microtubules. Though dependent on track curvature, the characteristic travel lengths of the microtubules on the tracks significantly exceeded earlier predictions. Moreover, we experimentally verified the performance of complex kinesin-1 patterns, recently designed by evolutionary algorithms for controlling the global directionality of microtubule motion on large-area substrates.

The simple and quick patterning of functional proteins on engineered surfaces affords an opportunity to fabricate protein microarrays in lab-on-chip systems. We report on the programmable patterning of proteins as well as the local activation of enzymes by visible light. We successfully generated functional protein patterns with different geometries in situ and demonstrated the specific patterning of multiple kinds of proteins side-by-side without the need for specific linker molecules or elaborate surface preparation.

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