ArticleNature communications2014
WT1 interacts with MAD2 and regulates mitotic checkpoint function.
Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 0 citations in OpenAlex.
- Review
- A novel WT1 gene mutation in a chinese girl with denys-drash syndrome.Journal of clinical laboratory analysis · 2021Article
- Moonlighting in Mitosis: Analysis of the Mitotic Functions of Transcription and Splicing Factors.Cells · 2020Review
- Wilms tumor 1 regulates lipid accumulation in human endometrial stromal cells during decidualization.The Journal of biological chemistry · 2020Article
- Identification of driver genes and key pathways of non-functional pituitary adenomas predicts the therapeutic effect of STO-609.PloS one · 2020Article
- Deficiency of PTEN leads to aberrant chromosome segregation through downregulation of MAD2.Molecular medicine reports · 2019Article
- Destabilization of spindle assembly checkpoint causes aneuploidy during meiosis II in murine post-ovulatory aged oocytes.The Journal of reproduction and development · 2019Article
- Wilms' tumor 1 drives fibroproliferation and myofibroblast transformation in severe fibrotic lung disease.JCI insight · 2018Article
- Regulation of AURORA B function by mitotic checkpoint protein MAD2.Cell cycle (Georgetown, Tex.) · 2016Article
- A role of WT1 in cell division and genomic stability.Cell cycle (Georgetown, Tex.) · 2015Review
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
Abstract
Tumour suppressors safeguard the fidelity of the mitotic checkpoint by transcriptional regulation of genes that encode components of the mitotic checkpoint complex (MCC). Here we report a new role for the tumour suppressor and transcription factor, WT1, in the mitotic checkpoint. We show that WT1 regulates the MCC by directly interacting with the spindle assembly checkpoint protein, MAD2. WT1 colocalizes with MAD2 during mitosis and preferentially binds to the functionally active, closed-conformer, C-MAD2. Furthermore, WT1 associates with the MCC containing MAD2, BUBR1 and CDC20, resulting in prolonged inhibition of the anaphase-promoting complex/cyclosome (APC/C) and delayed degradation of its substrates SECURIN and CYCLIN B1. Strikingly, RNA interference-mediated depletion of WT1 leads to enhanced turnover of SECURIN, decreased lag time to anaphase and defects in chromosome segregation. Our findings identify WT1 as a regulator of the mitotic checkpoint and chromosomal stability.
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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.