ArticleCell reports2026
CDK1-dependent N-terminal NuMA phosphorylation promotes dynein-dynactin-NuMA assembly for accurate chromosome segregation.
Article in Cell reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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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.
The trial behind it
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Who cites it
1 citing paper in PubMed.
- Activation and regulation of the dynein-dynactin-NuMA complex.Nature chemical biology · 2026Article
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Authors and funding
5 authors.
Funding
Abstract
The microtubule-based motor dynein and its cofactor dynactin are activated by various adaptors to fulfill essential functions throughout the cell cycle, including organelle transport and mitotic spindle assembly. NuMA is a mitotic adaptor that interacts with dynein-dynactin via its N-terminal region (NuMA-N). However, how NuMA-N binds and activates dynein-dynactin in mitosis remains unclear. Here, we combine a membrane-tethering assay, quantitative proteomics, and live-cell analyses to show that mitotic phosphorylation of NuMA-N drives dynein-dynactin-NuMA (DDN) assembly. We find that CDK1-Cyclin B1 phosphorylates NuMA-N, primarily at its conserved serine 203, which stimulates dynein activation in vitro. Replacing endogenous NuMA with phosphorylation-deficient mutants further reveals that NuMA-N phosphorylation, together with its dynein-binding site and Spindly-like motif, is required to form stable DDN complexes for functional spindle assembly. These results highlight CDK1-dependent N-terminal NuMA phosphorylation as a crucial mitotic phospho-switch that ensures stable multivalent interactions between dynein-dynactin and NuMA for accurate chromosome segregation.
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