ArticleThe Journal of cell biology2025
NuMA is a mitotic adaptor protein that activates dynein and connects it to microtubule minus ends.
Article in The Journal of cell biology, 2025. 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.
- Activation and regulation of the dynein-dynactin-NuMA complex.Nature chemical biology · 2026Article
- NuMA1 controls myonuclear motility in striated skeletal muscle through AMPK activity and is impaired in Duchenne muscular dystrophy.Cell death & disease · 2026Article
- CDK1-dependent N-terminal NuMA phosphorylation promotes dynein-dynactin-NuMA assembly for accurate chromosome segregation.Cell reports · 2026Article
- Motor-Assisted Co-Migration of Intracellular Organelles and Microtubules as a Mechanism for Directed Cargo Transport.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- Characterisation of the manchette architecture and its role as transport scaffold using cryo-electron tomography.Life science alliance · 2025Article
- An acentrosomal aster with atypical microtubule polarity recruits cytokinesis signals to its center in Xenopus egg extracts.Journal of cell science · 2025Article
- NuMA mechanically reinforces the spindle independently of its partner dynein.Current biology : CB · 2025Article
- Micron-scale protein transport along microtubules by kinesin-driven shepherding.bioRxiv : the preprint server for biology · 2025Article
- Molecular design principles for bipolar spindle organization by two opposing motors.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- NuMA mechanically reinforces the spindle independently of its partner dynein.bioRxiv : the preprint server for biology · 2024Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Nuclear mitotic apparatus protein (NuMA) is indispensable for the mitotic functions of the major microtubule minus-end directed motor cytoplasmic dynein 1. NuMA and dynein are both essential for correct spindle pole organization. How these proteins cooperate to gather microtubule minus ends at spindle poles remains unclear. Here, we use microscopy-based in vitro reconstitutions to demonstrate that NuMA is a dynein adaptor, activating processive dynein motility together with dynein's cofactors dynactin and Lissencephaly-1 (Lis1). Additionally, we find that NuMA binds and stabilizes microtubule minus ends, allowing dynein/dynactin/NuMA to transport microtubule minus ends as cargo to other minus ends. We further show that the microtubule-nucleating γ-tubulin ring complex (γTuRC) hinders NuMA binding and that NuMA only caps minus ends of γTuRC-nucleated microtubules after γTuRC release. These results provide new mechanistic insight into how dynein, dynactin, NuMA, and Lis1 together with γTuRC and uncapping proteins cooperate to organize spindle poles in cells.
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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.