Structural study of slective cargo transport by unconventional myosins

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The Cargo transportation by myosins is essential for proper cell phenomena. We peformed a series of structural and biochemicalstudies of the myosin-X tail domain , consisting of MyTH4 and FERM domains in complex with its specific cargo, a netrin receptor DCC (deleted in colorectal cancer). As the result, we found an unexpected binding mode of the DCC peptide, which is distinct from previously reported associations found in radixin/adhesion molecule complexes.Moreover, we revealed direct interactions between the MyTH4-FERM domain and tubulin C-terminal acidic tails, and identified a positively charged patch of the MyTH4 domain as a tubulin binding region. We also demonstrated that both DCC and integrin bindings interfere with microtubule binding and that DCC binding interferes with integrin binding. Our results provide the molecular basis by which myosin-X facilitates alternative dual binding to cargos and microtubules.