ArticleThe Journal of cell biology2025
Diverse microtubule-binding repeats regulate TPX2 activities at distinct locations within the spindle.
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 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.
- Light-induced spindle assembly through Aurora A clustering.EMBO reports · 2026Article
- Article
- Microtubule-Associated Proteins: From Dynamic Regulation of Microtubules to Cellular Architecture.Cells · 2026Review
- Identification of locally activated spindle-associated proteins in oocytes uncovers a phosphatase-driven mechanism.Journal of cell science · 2025Article
- How augmin establishes the angle of the microtubule branch site.Nature communications · 2025Article
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Authors and funding
5 authors.
Funding
Abstract
TPX2 is an elongated molecule containing multiple α-helical repeats. It stabilizes microtubules (MTs), promotes MT nucleation, and is essential for spindle assembly. However, the molecular basis of how TPX2 performs these functions remains elusive. Here, we systematically characterized the MT-binding activities of all TPX2 modules individually and in combinations and investigated their respective contributions both in vitro and in cells. We show that TPX2 contains α-helical repeats with opposite preferences for "extended" and "compacted" tubulin dimer spacing, and their distinct combinations produce divergent outcomes, making TPX2 activity highly robust yet tunable. Importantly, a repeat group at the C terminus, R8-9, is the key determinant of the TPX2 function. It stabilizes MTs by promoting rescues in vitro and is critical in spindle assembly. We propose a model where TPX2 activities are spatially regulated via its diverse MT-binding repeats to accommodate its varied functions in distinct locations within the spindle. Furthermore, we reveal a synergy between TPX2 and HURP in stabilizing spindle MTs.
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Registered trials
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