ArticleThe Journal of biological chemistry2010
Novel binding of the mitotic regulator TPX2 (target protein for Xenopus kinesin-like protein 2) to importin-alpha.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed, 89 citations in OpenAlex.
- Multiple roads between the nucleus and the cytoplasm: classes of linear NLSs and NESs and their receptors.Current opinion in structural biology · 2026Review
- The Chromatin Protein CFDP1 Activates TPX2 and Promotes Chromosomal Microtubule Nucleation and Spindle Assembly.International journal of molecular sciences · 2026Article
- The NLS3 Motif in TPX2 Regulates Spindle Architecture in Xenopus Egg Extracts.Cytoskeleton (Hoboken, N.J.) · 2026Article
- Alternative use of droxidopa for treating cervical cancer: inhibiting transferase, cell cycle signalling, and transport proteins via multitarget docking, DFT, MD simulations, and binding free energy studies.Medical oncology (Northwood, London, England) · 2025Article
- Evaluating the multitargeted potency of Pixuvri against cell cycle regulation proteins in cervical cancer.Frontiers in oncology · 2025Article
- HURP binding to the vinca domain of β-tubulin accounts for cancer drug resistance.Nature communications · 2024Article
- Unveiling the multitargeted repurposing potential of taxifolin (dihydroquercetin) in cervical cancer: an extensive MM\GBSA-based screening, and MD simulation study.Medical oncology (Northwood, London, England) · 2023Article
- Augmin is a Ran-regulated spindle assembly factor.The Journal of biological chemistry · 2023Article
- How Microtubules Build the Spindle Branch by Branch.Annual review of cell and developmental biology · 2022Review
- Differential recognition of canonical NF-κB dimers by Importin α3.Nature communications · 2022Article
- Diverse mechanisms regulate contractile ring assembly for cytokinesis in the two-cell Caenorhabditis elegans embryo.Journal of cell science · 2022Article
- Interaction of spindle assembly factor TPX2 with importins-α/β inhibits protein phase separation.The Journal of biological chemistry · 2021Article
- Complementary functions for the Ran gradient during division.Small GTPases · 2021Review
- A Ran-binding protein facilitates nuclear import of human papillomavirus type 16.PLoS pathogens · 2021Article
- Importin α phosphorylation promotes TPX2 activation by GM130 to control astral microtubules and spindle orientation.Journal of cell science · 2021Article
- Membrane and organelle dynamics during cell division.Nature reviews. Molecular cell biology · 2020Review
- Phase separation of TPX2 enhances and spatially coordinates microtubule nucleation.Nature communications · 2020Article
- Structural bioinformatics predicts that the Retinitis Pigmentosa-28 protein of unknown function FAM161A is a homologue of the microtubule nucleation factor Tpx2.F1000Research · 2020Article
- Phosphorylation of importin-α1 by CDK1-cyclin B1 controls mitotic spindle assembly.Journal of cell science · 2019Article
- Ran pathway-independent regulation of mitotic Golgi disassembly by Importin-α.Nature communications · 2019Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Several aspects of mitotic spindle assembly are orchestrated by the Ran GTPase through its modulation of the interaction between spindle assembly factors and importin-alpha. One such factor is TPX2 that promotes microtubule assembly in the vicinity of chromosomes. TPX2 is inhibited when bound to importin-alpha, which occurs when the latter is bound to importin-beta. The importin-alpha:beta interaction is disrupted by the high RanGTP concentration near the chromosomes, releasing TPX2. In more distal regions, where Ran is predominantly GDP-bound, TPX2 remains bound to importin-alpha and so is inhibited. Here we use a combination of structural and biochemical methods to define the basis for TPX2 binding to importin-alpha. A 2.2 A resolution crystal structure shows that the primary nuclear localization signal ((284)KRKH(287)) of TPX2, which has been shown to be crucial for inhibition, binds to the minor NLS-binding site on importin-alpha. This atypical interaction pattern was confirmed using complementary binding studies that employed importin-alpha variants in which binding to either the major or minor NLS-binding site was impaired, together with competition assays using the SV40 monopartite NLS that binds primarily to the major site. The different way in which TPX2 binds to importin-alpha could account for much of the selectivity necessary during mitosis because this would reduce the competition for binding to importin-alpha from other NLS-containing proteins.
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