title: The structure of the dynactin complex and its interaction with dynein.
abstract: Dynactin is an essential cofactor for the microtubule motor cytoplasmic dynein-1. We report the structure of the 23-subunit dynactin complex by cryo-electron microscopy to 4.0 angstroms. Our reconstruction reveals how dynactin is built around a filament containing eight copies of the actin-related protein Arp1 and one of β-actin. The filament is capped at each end by distinct protein complexes, and its length is defined by elongated peptides that emerge from the α-helical shoulder domain. A further 8.2 angstrom structure of the complex between dynein, dynactin, and the motility-inducing cargo adaptor Bicaudal-D2 shows how the translational symmetry of the dynein tail matches that of the dynactin filament. The Bicaudal-D2 coiled coil runs between dynein and dynactin to stabilize the mutually dependent interactions between all three components.
authors: Medical Research Council Laboratory of Molecular Biology, Division of Structural Studies, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
authors: Linas
authors: L
authors: Urnavicius
authors: Medical Research Council Laboratory of Molecular Biology, Division of Structural Studies, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
authors: Kai
authors: K
authors: Zhang
authors: Medical Research Council Laboratory of Molecular Biology, Division of Structural Studies, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
authors: Aristides G
authors: AG
authors: Diamant
authors: Medical Research Council Laboratory of Molecular Biology, Division of Structural Studies, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
authors: Carina
authors: C
authors: Motz
authors: Medical Research Council Laboratory of Molecular Biology, Division of Structural Studies, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
authors: Max A
authors: MA
authors: Schlager
authors: Medical Research Council Laboratory of Molecular Biology, Division of Structural Studies, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
authors: Minmin
authors: M
authors: Yu
authors: Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford OX1 3QZ, UK.
authors: Nisha A
authors: NA
authors: Patel
authors: Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, Oxford OX1 3QZ, UK.
authors: Carol V
authors: CV
authors: Robinson
authors: Medical Research Council Laboratory of Molecular Biology, Division of Structural Studies, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
authors: Andrew P
authors: AP
authors: Carter
mesh_terms: D000199:Actins / Q000737:chemistry; D000818:Animals; D020285:Cryoelectron Microscopy; D000072159:Dynactin Complex; D004398:Dyneins / Q000737:chemistry*; D006801:Humans; D051379:Mice; D008869:Microtubule-Associated Proteins / Q000737:chemistry*; D046912:Multiprotein Complexes / Q000737:chemistry*; D025941:Protein Interaction Mapping; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D021122:Protein Subunits / Q000737:chemistry; D013552:Swine
chemical_list: D000199:Actins; C561542:BICD2 protein, human; D000072159:Dynactin Complex; D008869:Microtubule-Associated Proteins; D046912:Multiprotein Complexes; D021122:Protein Subunits; D004398:Dyneins