ArticleCurrent biology : CB2025
NuMA mechanically reinforces the spindle independently of its partner dynein.
Article in Current biology : CB, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed.
- Activation and regulation of the dynein-dynactin-NuMA complex.Nature chemical biology · 2026Article
- Microtubule-Associated Proteins: From Dynamic Regulation of Microtubules to Cellular Architecture.Cells · 2026Review
- CDK1-dependent N-terminal NuMA phosphorylation promotes dynein-dynactin-NuMA assembly for accurate chromosome segregation.Cell reports · 2026Article
- Mechanical force locally damages, remodels, and stabilizes the lattice of spindle microtubules.Current biology : CB · 2026Article
- MBNL1-dependent alternative splicing promotes neuronal differentiation through regulation of NUMA1 exon 16 during fibroblast-to-neuron reprogramming.Frontiers in cell and developmental biology · 2026Article
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5 authors.
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Abstract
During cell division, both motor and non-motor proteins organize microtubules to build the spindle and maintain it against opposing forces. Nuclear mitotic apparatus (NuMA), a long microtubule-binding protein, is essential to spindle structure and function. NuMA recruits the motor dynein to actively cluster spindle microtubule minus-ends, but whether NuMA performs other spindle roles remains unknown. Here, we show that NuMA acts independently of dynein to passively reinforce the mammalian spindle. NuMA that cannot bind dynein is sufficient to protect spindle poles against fracture under external force. In contrast, NuMA with a shorter coiled coil or disrupted self-interactions cannot protect spindle poles, and NuMA turnover differences cannot explain mechanical differences. In vitro, NuMA's C terminus self-interacts and bundles microtubules without dynein, dependent on residues essential to pole protection in vivo. Together, this suggests that NuMA reinforces spindle poles by crosslinking microtubules, using its long coiled coil and self-interactions to reach multiple, far-reaching pole microtubules. We propose that NuMA acts as a mechanical "multitasker" targeting contractile motor activity and separately crosslinking microtubules, with both functions synergizing to drive spindle mechanical robustness.
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