ArticleThe Journal of cell biology2011
The N-terminal coiled-coil of Ndel1 is a regulated scaffold that recruits LIS1 to dynein.
Article in The Journal of cell biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 87 citations in OpenAlex.
- Nde1 promotes Lis1 binding to full-length autoinhibited human dynein 1.Nature chemical biology · 2026Article
- Cryo-EM captures early intermediate steps in dynein activation by LIS1.Nature communications · 2025Article
- CCSer2 gates dynein activity at the cell periphery.The Journal of cell biology · 2025Article
- Nde1 Promotes Lis1 Binding to Full-Length Autoinhibited Human Dynein-1.bioRxiv : the preprint server for biology · 2025Article
- The Role of Nde1 phosphorylation in interkinetic nuclear migration and neural migration during cortical development.Molecular biology of the cell · 2024Article
- CCSer2 gates dynein activity at the cell periphery.bioRxiv : the preprint server for biology · 2024Article
- Novel lissencephaly-associated NDEL1 variant reveals distinct roles of NDE1 and NDEL1 in nucleokinesis and human cortical malformations.Acta neuropathologica · 2024Article
- Nde1 promotes Lis1-mediated activation of dynein.Nature communications · 2023Article
- Conserved roles for the dynein intermediate chain and Ndel1 in assembly and activation of dynein.Nature communications · 2023Article
- Nde1 Promotes Lis1-Mediated Activation of Dynein.bioRxiv : the preprint server for 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
- Aurora A phosphorylates Ndel1 to reduce the levels of Mad1 and NuMA at spindle poles.Molecular biology of the cell · 2023Article
- Article
- Sequential accumulation of dynein and its regulatory proteins at the spindle region in the Caenorhabditis elegans embryo.Scientific reports · 2022Article
- Nde1 and Ndel1: Outstanding Mysteries in Dynein-Mediated Transport.Frontiers in cell and developmental biology · 2022Review
- Structure and Mechanics of Dynein Motors.Annual review of biophysics · 2021Review
- Arsenic trioxide disturbs the LIS1/NDEL1/dynein microtubule dynamic complex by disrupting the CLIP170 zinc finger in head and neck cancer.Toxicology and applied pharmacology · 2020Article
- Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Ndel1 has been implicated in a variety of dynein-related processes, but its specific function is unclear. Here we describe an experimental approach to evaluate a role of Ndel1 in dynein-dependent microtubule self-organization using Ran-mediated asters in meiotic Xenopus egg extracts. We demonstrate that extracts depleted of Ndel1 are unable to form asters and that this defect can be rescued by the addition of recombinant N-terminal coiled-coil domain of Ndel1. Ndel1-dependent microtubule self-organization requires an interaction between Ndel1 and dynein, which is mediated by the dimerization fragment of the coiled-coil. Full rescue by the coiled-coil domain requires LIS1 binding, and increasing LIS1 concentration partly rescues aster formation, suggesting that Ndel1 is a recruitment factor for LIS1. The interactions between Ndel1 and its binding partners are positively regulated by phosphorylation of the unstructured C terminus. Together, our results provide important insights into how Ndel1 acts as a regulated scaffold to temporally and spatially regulate dynein.
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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.