Abstract
Dynein adapters such as Bicaudal D2 are key players in dynein-dependent transport, as they recognize cargo, link them to the motor complex and are also required to activate dynein for processive motility. BicD recruits dynein to Rab6, which is embedded in secretory and Golgi-derived vesicles, to facilitate their minus-end directed transport. The molecular mechanism of how BicD2 recognizes Rab6 is elusive. Here, we characterize Rab6 mutants that diminish binding to BicD2 by biophysical methods, including circular dichroism spectroscopy. Similar as observed for Nup358, the Rab6GTP region that binds to BicD2 is intrinsically disordered, and we propose that it transitions from a random coil conformation to a cargo-recognition alpha-helix in the BicD2/Rab6GTP complex. Our results provide insights into the molecular mechanism of cargo selection of BicD2, which facilitates transport pathways that are important for brain development, transport of Golgi derived vesicles and faithful chromosome segregation.
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