ArticleProceedings of the National Academy of Sciences of the United States of America2006
Rae1 interaction with NuMA is required for bipolar spindle formation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
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Who cites it
66 citing papers in PubMed, 97 citations in OpenAlex.
- Unraveling dynamics of nuclear pore and chromatin via HS-AFM.Anatomical science international · 2026Review
- Review
- Advances in the understanding of nuclear pore complexes in human diseases.Journal of cancer research and clinical oncology · 2024Review
- The response of Dual-leucine zipper kinase (DLK) to nocodazole: Evidence for a homeostatic cytoskeletal repair mechanism.PloS one · 2024Article
- Systems-level analyses of protein-protein interaction network dysfunctions via epichaperomics identify cancer-specific mechanisms of stress adaptation.Nature communications · 2023Article
- The pediatric leukemia oncoprotein NUP98-KDM5A induces genomic instability that may facilitate malignant transformation.Cell death & disease · 2023Article
- Novel Prediction Method Applied to Wound Age Estimation: Developing a Stacking Ensemble Model to Improve Predictive Performance Based on Multi-mRNA.Diagnostics (Basel, Switzerland) · 2023Article
- SUN2 regulates mitotic duration in response to extracellular matrix rigidity.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- SARS-CoV-2 ORF6 disrupts innate immune signalling by inhibiting cellular mRNA export.PLoS pathogens · 2022Article
- New Activities of the Nuclear Pore Complexes.Cells · 2021Article
- Mitotic checkpoint regulator RAE1 promotes tumor growth in colorectal cancer.Cancer science · 2021Article
- Ribonucleic Acid Export 1 Is a Kinetochore-Associated Protein That Participates in Chromosome Alignment in Mouse Oocytes.International journal of molecular sciences · 2021Article
- The Nuclear Mitotic Apparatus (NuMA) Protein: A Key Player for Nuclear Formation, Spindle Assembly, and Spindle Positioning.Frontiers in cell and developmental biology · 2021Review
- Differential turnover of Nup188 controls its levels at centrosomes and role in centriole duplication.The Journal of cell biology · 2020Article
- RAE1 promotes BMAL1 shuttling and regulates degradation and activity of CLOCK: BMAL1 heterodimer.Cell death & disease · 2019Article
- Nucleoporin Nup58 localizes to centrosomes and mid-bodies during mitosis.Cell division · 2019Article
- Article
- The mitotic checkpoint regulator RAE1 induces aggressive breast cancer cell phenotypes by mediating epithelial-mesenchymal transition.Scientific reports · 2017Article
- B-type nuclear lamin and the nuclear pore complex Nup107-160 influences maintenance of the spindle envelope required for cytokinesis in Drosophila male meiosis.Biology open · 2016Article
- The Hippo Pathway Targets Rae1 to Regulate Mitosis and Organ Size and to Feed Back to Regulate Upstream Components Merlin, Hippo, and Warts.PLoS genetics · 2016Article
6 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In eukaryotic cells, the faithful segregation of daughter chromosomes during cell division depends on formation of a microtubule (MT)-based bipolar spindle apparatus. The Nuclear Mitotic Apparatus protein (NuMA) is recruited from interphase nuclei to spindle MTs during mitosis. The carboxy terminal domain of NuMA binds MTs, allowing a NuMA dimer to function as a "divalent" crosslinker that bundles MTs. The messenger RNA export factor, Rae1, also binds to MTs. Lowering Rae1 or increasing NuMA levels in cells results in spindle abnormalities. We have identified a mitotic-specific interaction between Rae1 and NuMA and have explored the relationship between Rae1 and NuMA in spindle formation. We have mapped a specific binding site for Rae1 on NuMA that would convert a NuMA dimer to a "tetravalent" crosslinker of MTs. In mitosis, reducing Rae1 or increasing NuMA concentration would be expected to alter the valency of NuMA toward MTs; the "density" of NuMA-MT crosslinks in these conditions would be diminished, even though a threshold number of crosslinks sufficient to stabilize aberrant multipolar spindles may form. Consistent with this interpretation, we found that coupling NuMA overexpression to Rae1 overexpression or coupling Rae1 depletion to NuMA depletion prevented the formation of aberrant spindles. Likewise, we found that overexpression of the specific Rae1-binding domain of NuMA in HeLa cells led to aberrant spindle formation. These data point to the Rae1-NuMA interaction as a critical element for normal spindle formation in mitosis.
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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.