ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2006
Regulation of cytoplasmic dynein ATPase by Lis1.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 76 citations in OpenAlex.
- Expanding the clinical phenotype of DYNC1H1 -associated mutations: a Chinese family with autosomal dominant complex hereditary spastic paraplegia.BMC medical genomics · 2025Article
- Multiple steps of dynein activation by Lis1 visualized by cryo-EM.Nature structural & molecular biology · 2025Article
- Pt-LIS1 participates nuclear deformation and acrosome formation via regulating Dynein-1 during spermatogenesis in Portunus trituberculatus.Scientific reports · 2025Article
- LIS1 and NDEL1 Regulate Axonal Trafficking of Mitochondria in Mature Neurons.Frontiers in molecular neuroscience · 2022Article
- Article
- Activation and Regulation of Cytoplasmic Dynein.Trends in biochemical sciences · 2020Review
- Cargo-Mediated Activation of Cytoplasmic DyneinFrontiers in cell and developmental biology · 2020Review
- Insulin signaling regulates a functional interaction between adenomatous polyposis coli and cytoplasmic dynein.Molecular biology of the cell · 2017Article
- N-Acetyl-D-Glucosamine Kinase Interacts with Dynein-Lis1-NudE1 Complex and Regulates Cell Division.Molecules and cells · 2016Article
- GSK-3β Phosphorylation of Cytoplasmic Dynein Reduces Ndel1 Binding to Intermediate Chains and Alters Dynein Motility.Traffic (Copenhagen, Denmark) · 2015Article
- Article
- Nudel/NudE and Lis1 promote dynein and dynactin interaction in the context of spindle morphogenesis.Molecular biology of the cell · 2013Article
- Muscle length and myonuclear position are independently regulated by distinct Dynein pathways.Development (Cambridge, England) · 2012Article
- Association of Lis1 with outer arm dynein is modulated in response to alterations in flagellar motility.Molecular biology of the cell · 2012Article
- A mouse neurodegenerative dynein heavy chain mutation alters dynein motility and localization in Neurospora crassa.Cytoskeleton (Hoboken, N.J.) · 2012Article
- Lis1 acts as a "clutch" between the ATPase and microtubule-binding domains of the dynein motor.Cell · 2012Article
- Analyses of dynein heavy chain mutations reveal complex interactions between dynein motor domains and cellular dynein functions.Genetics · 2012Article
- Regulation of dynein localization and centrosome positioning by Lis-1 and asunder during Drosophila spermatogenesis.Development (Cambridge, England) · 2012Article
- Lis1 is an initiation factor for dynein-driven organelle transport.The Journal of cell biology · 2012Article
- Ndel1-derived peptides modulate bidirectional transport of injected beads in the squid giant axon.Biology open · 2012Article
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
Mutations in Lis1 cause classical lissencephaly, a developmental brain abnormality characterized by defects in neuronal positioning. Over the last decade, a clear link has been forged between Lis1 and the microtubule motor cytoplasmic dynein. Substantial evidence indicates that Lis1 functions in a highly conserved pathway with dynein to regulate neuronal migration and other motile events. Yeast two-hybrid studies predict that Lis1 binds directly to dynein heavy chains (Sasaki et al., 2000; Tai et al., 2002), but the mechanistic significance of this interaction is not well understood. We now report that recombinant Lis1 binds to native brain dynein and significantly increases the microtubule-stimulated enzymatic activity of dynein in vitro. Lis1 does this without increasing the proportion of dynein that binds to microtubules, indicating that Lis1 influences enzymatic activity rather than microtubule association. Dynein stimulation in vitro is not a generic feature of microtubule-associated proteins, because tau did not stimulate dynein. To our knowledge, this is the first indication that Lis1 or any other factor directly modulates the enzymatic activity of cytoplasmic dynein. Lis1 must be able to homodimerize to stimulate dynein, because a C-terminal fragment (containing the dynein interaction site but missing the self-association domain) was unable to stimulate dynein. Binding and colocalization studies indicate that Lis1 does not interact with all dynein complexes found in the brain. We propose a model in which Lis1 stimulates the activity of a subset of motors, which could be particularly important during neuronal migration and long-distance axonal transport.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.