ArticlebioRxiv : the preprint server for biology2025
Cargo adaptors use a handhold mechanism to engage with myosin V for organelle transport.
Article in bioRxiv : the preprint server for biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Myo2, a myosin V motor, is essential for organelle transport in budding yeast. Its attachment to and detachment from cargo are mediated by adaptor molecules. Vac17, a vacuole-specific adaptor, links Myo2 to Vac8 on the vacuole membrane, and plays a key role in the formation and dissociation of the Myo2-Vac17-Vac8 complex. Using genetics, cryo-electron microscopy and structure prediction, we find that Vac17 interacts with Myo2 through two distinct sites rather than a single interface. Similarly, the peroxisome adapter Inp2 engages two separate regions of Myo2, one of which overlaps with Vac17. These findings support a "handhold" model, in which cargo adaptors occupy multiple sites on the Myo2 tail, enhancing motor-cargo interactions and likely providing additional regulatory control over motor recruitment.
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