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Myosin V (MyoV) motors have been implicated in the intracellular transport of diverse cargoes including vesicles, organelles, RNA-protein complexes, and regulatory proteins. Here, we have solved the cargo-binding domain (CBD) structures of the three human MyoV paralogs (Va, Vb, and Vc), revealing subtle structural changes that drive functional differentiation and a novel redox mechanism controlling the CBD dimerization process, which is unique for the MyoVc subclass. Moreover, the cargo- and motor-binding sites were structurally assigned, indicating the conservation of residues involved in the recognition of adaptors for peroxisome transport and providing high resolution insights into motor domain inhibition by CBD. These results contribute to understanding the structural requirements for cargo transport, autoinhibition, and regulatory mechanisms in myosin V motors.

Original publication

DOI

10.1074/jbc.M113.507202

Type

Journal article

Journal

J Biol Chem

Publication Date

22/11/2013

Volume

288

Pages

34131 - 34145

Keywords

Cargo-binding Domain, Cell Signaling, Crystal Structure, Intracellular Trafficking, Molecular Motors, Molecular Plasticity, Myosin, Myosin V, Redox Dimerization, Binding Sites, Biological Transport, Active, Humans, Myosin Type V, Peroxisomes, Protein Structure, Quaternary, Protein Structure, Tertiary, Structural Homology, Protein