Key result
Myosin X post-IQ tail biases head orientation to enable selective processive runs on fascin-actin bundles.
The structured post-IQ domain of myosin X is critical for its selectivity in transporting components along bundled actin filaments.
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Should not change clinical practice; hypothesis-generating for myosin X selectivity in actin transport.
Without guidance cues, cytoskeletal motors would traffic components to the wrong destination with disastrous consequences for the cell. Recently, we identified a motor protein, myosin X, that identifies bundled actin filaments for transport. These bundles direct myosin X to a unique destination, the tips of cellular filopodia. Because the structural and kinetic features that drive bundle selection are unknown, we employed a domain-swapping approach with the nonselective myosin V to identify the selectivity module of myosin X. We found a surprising role of the myosin X tail region (post-IQ) in supporting long runs on bundles. Moreover, the myosin X head is adapted for initiating processive runs on bundles. We found that the tail is structured and biases the orientation of the two myosin X heads because a targeted insertion that introduces flexibility in the tail abolishes selectivity. Together, these results suggest how myosin motors may manage to read cellular addresses.
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Nagy et al. (2010) studied this question. Domain-swapping approach with nonselective myosin V was evaluated on Selectivity of myosin X for fascin-actin bundles. The structured post-IQ tail region of myosin X biases the orientation of its two heads, enabling selective processive runs on fascin-actin bundles.
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