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- W2970520110 abstract "Dynein-2 assembles with polymeric intraflagellar transport (IFT) trains to form a transport machinery that is crucial for cilia biogenesis and signaling. Here we recombinantly expressed the ~1.4-MDa human dynein-2 complex and solved its cryo-EM structure to near-atomic resolution. The two identical copies of the dynein-2 heavy chain are contorted into different conformations by a WDR60-WDR34 heterodimer and a block of two RB and six LC8 light chains. One heavy chain is steered into a zig-zag conformation, which matches the periodicity of the anterograde IFT-B train. Contacts between adjacent dyneins along the train indicate a cooperative mode of assembly. Removal of the WDR60-WDR34-light chain subcomplex renders dynein-2 monomeric and relieves autoinhibition of its motility. Our results converge on a model in which an unusual stoichiometry of non-motor subunits controls dynein-2 assembly, asymmetry, and activity, giving mechanistic insight into the interaction of dynein-2 with IFT trains and the origin of diverse functions in the dynein family." @default.
- W2970520110 created "2019-09-05" @default.
- W2970520110 creator A5012194078 @default.
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- W2970520110 creator A5064994399 @default.
- W2970520110 creator A5071533128 @default.
- W2970520110 creator A5082438989 @default.
- W2970520110 date "2019-08-26" @default.
- W2970520110 modified "2023-10-16" @default.
- W2970520110 title "Structure of the dynein-2 complex and its assembly with intraflagellar transport trains" @default.
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- W2970520110 doi "https://doi.org/10.1038/s41594-019-0286-y" @default.
- W2970520110 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6774794" @default.
- W2970520110 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31451806" @default.
- W2970520110 hasPublicationYear "2019" @default.
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