ArticleNature structural & molecular biology2023
Microtubule-binding-induced allostery triggers LIS1 dissociation from dynein prior to cargo transport.
Article in Nature structural & molecular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Article
- A nucleotide code governs Lis1's ability to relieve dynein autoinhibition.Nature chemical biology · 2026Article
- Adaptor-mediated recruitment of three dyneins to dynactin enhances force generation.Nature cell biology · 2026Article
- Cancer Stem Cells Shift Metabolite Acetyl-Coenzyme A to Abrogate the Differentiation of CD103Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Nde1 promotes Lis1 binding to full-length autoinhibited human dynein 1.Nature chemical biology · 2026Article
- Structural and ensemble-based mechanistic insights into cytoplasmic dynein-1.Frontiers in molecular biosciences · 2026Review
- The mechanochemical cycle of reactive full-length human dynein 1.Nature structural & molecular biology · 2025Article
- Cryo-EM captures early intermediate steps in dynein activation by LIS1.Nature communications · 2025Article
- Multiple steps of dynein activation by Lis1 visualized by cryo-EM.Nature structural & molecular biology · 2025Article
- Nde1 Promotes Lis1 Binding to Full-Length Autoinhibited Human Dynein-1.bioRxiv : the preprint server for biology · 2025Article
- Lis1 slows force-induced detachment of cytoplasmic dynein from microtubules.Nature chemical biology · 2024Article
- Molecular mechanism of dynein-dynactin complex assembly by LIS1.Science (New York, N.Y.) · 2024Article
- Cryo-EM reveals how the mastigoneme assembles and responds to environmental signal changes.The Journal of cell biology · 2023Article
- Conserved roles for the dynein intermediate chain and Ndel1 in assembly and activation of dynein.Nature communications · 2023Article
- New pieces for the Lis1-dynein puzzle.Nature structural & molecular biology · 2023Article
- Ndel1 disfavors dynein-dynactin-adaptor complex formation in two distinct ways.The Journal of biological chemistry · 2023Article
- Ndel1 modulates dynein activation in two distinct ways.bioRxiv : the preprint server for biology · 2023Article
- Conserved Roles for the Dynein Intermediate Chain and Ndel1 in Assembly and Activation of Dynein.bioRxiv : the preprint server for biology · 2023Article
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Authors and funding
9 authors.
Funding
Abstract
The lissencephaly-related protein LIS1 is a critical regulator of cytoplasmic dynein that governs motor function and intracellular localization (for example, to microtubule plus-ends). Although LIS1 binding is required for dynein activity, its unbinding prior to initiation of cargo transport is equally important, since preventing dissociation leads to dynein dysfunction. To understand whether and how dynein-LIS1 binding is modulated, we engineered dynein mutants locked in a microtubule-bound (MT-B) or microtubule-unbound (MT-U) state. Whereas the MT-B mutant exhibits low LIS1 affinity, the MT-U mutant binds LIS1 with high affinity, and as a consequence remains almost irreversibly associated with microtubule plus-ends. We find that a monomeric motor domain is sufficient to exhibit these opposing LIS1 affinities, and that this is evolutionarily conserved between yeast and humans. Three cryo-EM structures of human dynein with and without LIS1 reveal microtubule-binding induced conformational changes responsible for this regulation. Our work reveals key biochemical and structural insight into LIS1-mediated dynein activation.
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