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Slip sliding away with myosin V

Life is complicated. Things would be much simpler for myosin V if it had to contend only with the in vitro environments created to facilitate elucidation of its mechanochemical properties: isolated actin filament tracks with simple geometries, minimal physical barriers to movement, and no need to interface with microtubule motors that normally cooperate with it (1). But in the cell, myosin V must deal with actin filament networks composed of randomly oriented and/or branched filaments, numerous physical barriers to movement of its vesicular cargo, and the necessity to work in a coordinated fashion with plus-end-directed microtubule motors in a partnership that couples long-range vesicle movement on microtubules with short-range actin-based movement by myosin V in the cell periphery (2, 3). In the paper by Ali et al. in a recent issue of PNAS (4), the authors have begun to tackle this complexity by designing in vitro motility assays in which myosin V encounters either intersecting/branched actin filaments or actin–microtubule intersections. The results are both informative and surprising.