ArticleThe Journal of biological chemistry2021
Interaction of spindle assembly factor TPX2 with importins-α/β inhibits protein phase separation.
Article in The Journal of biological chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
22 citing papers in PubMed, 28 citations in OpenAlex.
- MORC1 coordinates TRIM28 interaction and nuclear condensate formation for transposon silencing.iScience · 2026Article
- Noncentrosomal Microtubule Assembly and Its Regulation.Cytoskeleton (Hoboken, N.J.) · 2026Review
- Distinguishing near- versus off-critical phase behaviors of intrinsically disordered proteins.Reports on progress in physics. Physical Society (Great Britain) · 2026Article
- The NLS3 Motif in TPX2 Regulates Spindle Architecture in Xenopus Egg Extracts.Cytoskeleton (Hoboken, N.J.) · 2026Article
- Diverse microtubule-binding repeats regulate TPX2 activities at distinct locations within the spindle.The Journal of cell biology · 2025Article
- Phase separation of microtubule-binding proteins - implications for neuronal function and disease.Journal of cell science · 2024Review
- Exploring the Blood Biomarkers and Potential Therapeutic Agents for Human Acute Mountain Sickness Based on Transcriptomic Analysis, Inflammatory Infiltrates and Molecular Docking.International journal of molecular sciences · 2024Article
- Liquid-liquid phase separation of microtubule-binding proteins in the regulation of spindle assembly.Cell proliferation · 2024Review
- Programmable de novo designed coiled coil-mediated phase separation in mammalian cells.Nature communications · 2023Article
- Abl2 repairs microtubules and phase separates with tubulin to promote microtubule nucleation.Current biology : CB · 2023Article
- Phase Transitions of Associative Biomacromolecules.Chemical reviews · 2023Review
- Microtubule binding of the human augmin complex is directly controlled by importins and Ran-GTP.Journal of cell science · 2023Article
- Co-translational binding of importins to nascent proteins.Nature communications · 2023Article
- Role of the TPX2/NCOA5 axis in regulating proliferation, migration, invasion and angiogenesis of breast cancer cells.Experimental and therapeutic medicine · 2023Article
- Augmin is a Ran-regulated spindle assembly factor.The Journal of biological chemistry · 2023Article
- Integrated model of the vertebrate augmin complex.Nature communications · 2023Article
- Ran GTPase and Its Importance in Cellular Signaling and Malignant Phenotype.International journal of molecular sciences · 2023Review
- Genome-wide analysis ofFrontiers in plant science · 2023Article
- How Microtubules Build the Spindle Branch by Branch.Annual review of cell and developmental biology · 2022Review
- Differential nuclear import sets the timing of protein access to the embryonic genome.Nature communications · 2022Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The microtubule-based mitotic spindle is responsible for equally partitioning the genome during each cell division, and its assembly is executed via several microtubule nucleation pathways. Targeting Protein for XKlp2 (TPX2) stimulates the branching microtubule nucleation pathway, where new microtubules are nucleated from preexisting ones within mitotic or meiotic spindles. TPX2, like other spindle assembly factors, is sequestered by binding to nuclear importins-α/β until the onset of mitosis, yet the molecular nature of this regulation remains unclear. Here we demonstrate that TPX2 interacts with importins-α/β with nanomolar affinity in a 1:1:1 monodispersed trimer. We also identify a new nuclear localization sequence in TPX2 that contributes to its high-affinity interaction with importin-α. In addition, we establish that TPX2 interacts with importin-β via dispersed, weak interactions. We show that interactions of both importin-α and -β with TPX2 inhibit its ability to undergo phase separation, which was recently shown to enhance the kinetics of branching microtubule nucleation. In summary, our study informs how importins regulate TPX2 to facilitate spindle assembly, and provides novel insight into the functional regulation of protein phase separation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.