title: Antiparallel coiled-coil-mediated dimerization of myosin X.
abstract: Processive movements of unconventional myosins on actin filaments generally require motor dimerization. A commonly accepted myosin dimerization mechanism is via formation of a parallel coiled-coil dimer by a stretch of amino acid residues immediately carboxyl-terminal to the motor's lever-arm domain. Here, we discover that the predicted coiled-coil region of myosin X forms a highly stable, antiparallel coiled-coil dimer (anti-CC). Disruption of the anti-CC either by single-point mutations or by replacement of the anti-CC with a parallel coiled coil with a similar length compromised the filopodial induction activity of myosin X. We further show that the anti-CC and the single α-helical domain of myosin X are connected by a semirigid helical linker. The anti-CC-mediated dimerization may enable myosin X to walk on both single and bundled actin filaments.
authors.affiliation: Division of Life Science, State Key Laboratory of Molecular Neuroscience and Center of Systems Biology and Human Health, School of Science and Institute for Advanced Study,  Hong Kong University of Science and Technology, Kowloon, Hong Kong,  China.
authors.forename: Qing
authors.initials: Q
authors.lastname: Lu
authors.forename: Fei
authors.initials: F
authors.lastname: Ye
authors.forename: Zhiyi
authors.initials: Z
authors.lastname: Wei
authors.forename: Zilong
authors.initials: Z
authors.lastname: Wen
authors.forename: Mingjie
authors.initials: M
authors.lastname: Zhang
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D019281:Dimerization; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009218:Myosins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
chemical_list: C498718:MYO10 protein, human; D009218:Myosins