Cooperative molecular motors moving back and forth.

We use a two-state ratchet model to study the cooperative bidirectional motion of molecular motors on cytoskeletal tracks with randomly alternating polarities. Our model is based on a previously proposed model [Badoual, Proc. Natl. Acad. Sci. U.S.A. 99, 6696 (2002)] for collective motor dynamics and, in addition, takes into account the cooperativity effect arising from the elastic tension that develops in the cytoskeletal track due to the joint action of the walking motors. We show, both computationally and analytically, that this additional cooperativity effect leads to a dramatic reduction in the characteristic reversal time of the bidirectional motion, especially in systems with a large number of motors. We also find that bidirectional motion takes place only on (almost) apolar tracks, while on even slightly polar tracks the cooperative motion is unidirectional. We argue that the origin of these observations is the sensitive dependence of the cooperative dynamics on the difference between the number of motors typically working in and against the instantaneous direction of motion.

The fusion of actin bundles driven by interacting motor proteins.

The cooperative action of many molecular motors is essential for dynamic processes such as cell motility and mitosis. This action can be studied by using motility assays which track the motion of cytoskeletal filaments over a surface coated with motor proteins. Here, we propose to use a motility assay consisting of a-polar actin bundles subjected to the action of myosin II motors where no external loading is applied. In this work we focus on those bundles undergoing fusion with other nearby bundles. Specifically, we investigate the role of the bundles' dimension on the transition from bidirectional to directional motion and on the properties of their motion during fusion. Our experimental data reveal that only small bundles exhibit dynamic transition to directional motion, implying that the forces acting on them exceed the threshold value necessary to induce the transition. Moreover, these bundles accelerate along their trajectory, suggesting that the forces acting on them increase while approaching each other. We show that these forces do not originate from external loading but rather arise from the action of the motors on the bundles. These forces are transmitted through the medium over micron-scale distances without being cut off. Moreover, we show that the forces propagate to distances that are proportional to the size of the bundles, or equivalently, to the number of motors, which they interact with.

A cytoskeletal demolition worker: myosin II acts as an actin depolymerization agent.

Myosin II motors play several important roles in a variety of cellular processes, some of which involve active assembly/disassembly of cytoskeletal substructures. Myosin II motors have been shown to function in actin bundle turnover in neuronal growth cones and in the recycling of actin filaments during cytokinesis. Close examination had shown an intimate relationship between myosin II motor adenosine triphosphatase activity and actin turnover rate. However, the direct implication of myosin II in actin turnover is still not understood. Herein, we show, using high-resolution cryo-transmission electron microscopy, that myosin II motors control the turnover of actin bundles in a concentration-dependent manner in vitro. We demonstrate that disassembly of actin bundles occurs through two main stages: the first stage involves unbundling into individual filaments, and the second involves their subsequent depolymerization. These evidence suggest that, in addition to their "classical" contractile abilities, myosin II motors may be directly implicated in active actin depolymerization. We believe that myosin II motors may function similarly in vivo (e.g., in the disassembly of the contractile ring by fine tuning the local concentration/activity of myosin II motors).