ArticleMolecular biology of the cell2020
Conformational diversity of dynactin sidearm and domain organization of its subunit p150.
Article in Molecular biology of the cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Microtubule architecture connects AMOT stability to YAP/TAZ mechanotransduction and Hippo signalling.Nature cell biology · 2025Article
- VezA/vezatin facilitates proper assembly of the dynactin complex in vivo.Cell reports · 2024Article
- Autophagy initiation triggers p150Cellular and molecular life sciences : CMLS · 2024Article
- VezA/vezatin facilitates proper assembly of the dynactin complex in vivo.bioRxiv : the preprint server for biology · 2024Article
- Molecular mechanism of dynein-dynactin complex assembly by LIS1.Science (New York, N.Y.) · 2024Article
- Conserved roles for the dynein intermediate chain and Ndel1 in assembly and activation of dynein.Nature communications · 2023Article
- Conserved Roles for the Dynein Intermediate Chain and Ndel1 in Assembly and Activation of Dynein.bioRxiv : the preprint server for biology · 2023Article
- Cryo-EM reveals the complex architecture of dynactin's shoulder region and pointed end.The EMBO journal · 2021Article
- Distinct retrograde microtubule motor sets drive early and late endosome transport.The EMBO journal · 2020Article
- Cargo-Mediated Activation of Cytoplasmic DyneinFrontiers in cell and developmental biology · 2020Review
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Authors and funding
9 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Dynactin is a principal regulator of the minus-end directed microtubule motor dynein. The sidearm of dynactin is essential for binding to microtubules and regulation of dynein activity. Although our understanding of the structure of the dynactin backbone (Arp1 rod) has greatly improved recently, structural details of the sidearm subcomplex remain elusive. Here, we report the flexible nature and diverse conformations of dynactin sidearm observed by electron microscopy. Using nanogold labeling and deletion mutant analysis, we determined the domain organization of the largest subunit p150 and discovered that its coiled-coil (CC1), dynein-binding domain, adopted either a folded or an extended form. Furthermore, the entire sidearm exhibited several characteristic forms, and the equilibrium among them depended on salt concentrations. These conformational diversities of the dynactin complex provide clues to understanding how it binds to microtubules and regulates dynein.
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