Structural basis of myosin V Rab GTPase-dependent cargo recognition

Significance

Directed movement is essential for life, and cytoskeleton-based motors generate mechanical force and motion to precisely organize the cell. Their selective recruitment and activation at particular times and positions in cells is critical to numerous cell processes. This paper provides unique insights into the specific recognition of cellular compartments by the myosin V nanomotor via direct or indirect interactions with Rab GTPases. These studies highlight the role of plasticity in the binding site to achieve selectivity in cargo/motor recognition. We also describe how the globular tail domain sequence of the motor diverged among isoforms during evolution to maintain core shared functions while promoting diversification of cellular roles by acquiring new specific partner interactions.