ArticleNature chemical biology2026
Activation and regulation of the dynein-dynactin-NuMA complex.
Article in Nature chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- A TerminaTOR of mTORC1 signaling.Nature chemical biology · 2026Article
- CDK1-dependent N-terminal NuMA phosphorylation promotes dynein-dynactin-NuMA assembly for accurate chromosome segregation.Cell reports · 2026Article
- Structural and ensemble-based mechanistic insights into cytoplasmic dynein-1.Frontiers in molecular biosciences · 2026Review
- Review
- 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
- NuMA is a mitotic adaptor protein that activates dynein and connects it to microtubule minus ends.The Journal of cell biology · 2025Article
- NuMA mechanically reinforces the spindle independently of its partner dynein.bioRxiv : the preprint server for biology · 2024Article
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Authors and funding
11 authors.
Funding
Abstract
During cell division, the nuclear mitotic apparatus protein (NuMA) orchestrates the focusing of microtubule minus-ends in spindle poles and cortical force generation on astral microtubules by interacting with dynein motors, microtubules and other cellular factors. Here we used in vitro reconstitution, cryo-electron microscopy and live-cell imaging to understand the mechanism and regulation of NuMA. We determined the structure of the processive dynein-dynactin-NuMA complex (DDN) and showed that the NuMA N terminus drives dynein motility in vitro and facilitates dynein-mediated transport in live cells. The C terminus of NuMA directly binds and suppresses the dynamics of the microtubule minus-end. Full-length NuMA is autoinhibited for its interactions with dynein and microtubules, whereas mitotically phosphorylated NuMA activates dynein in vitro and interphase cells. Together with dynein, activated full-length NuMA focuses microtubule minus-ends into aster-like structures. These results provide critical insights into the activation of NuMA and dynein for their mitotic functions.
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Registered trials
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