ArticleGenes & development1998
Inhibition of cellular proliferation by the Wilms tumor suppressor WT1 requires association with the inducible chaperone Hsp70.
Article in Genes & development, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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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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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
23 citing papers in PubMed, 96 citations in OpenAlex.
- WT1 gene: a potential therapeutic target for multiple cancer treatment strategies.Clinical and experimental medicine · 2025Review
- Heat-shock-induced tyrosinase gene ablation with CRISPR in zebrafish.Molecular genetics and genomics : MGG · 2020Article
- Heat shock protein 70/nitric oxide effect on stretched tubular epithelial cells linked to WT-1 cytoprotection during neonatal obstructive nephropathy.International urology and nephrology · 2017Article
- Growing evidence suggests WT1 effects in the kidney development are modulated by Hsp70/NO interaction.Journal of nephrology · 2017Review
- Changes in renal WT-1 expression preceding hypertension development.BMC nephrology · 2016Article
- Mediators and mechanisms of heat shock protein 70 based cytoprotection in obstructive nephropathy.Cell stress & chaperones · 2015Review
- Systems biology approach to studying proliferation-dependent prognostic subnetworks in breast cancer.Scientific reports · 2015Article
- Mechanisms of transcriptional regulation by WT1 (Wilms' tumour 1).The Biochemical journal · 2014Review
- Wt-1 Expression Linked to Nitric Oxide Availability during Neonatal Obstructive Nephropathy.Advances in urology · 2013Review
- Heat shock protein 90 regulates the expression of Wilms tumor 1 protein in myeloid leukemias.Blood · 2010Article
- HtrA2, taming the oncogenic activities of WT1.Cell cycle (Georgetown, Tex.) · 2010Article
- In silico regulatory analysis for exploring human disease progression.Biology direct · 2008Article
- A tumor suppressor and oncogene: the WT1 story.Leukemia · 2007Review
- HSP70 induction by ING proteins sensitizes cells to tumor necrosis factor alpha receptor-mediated apoptosis.Molecular and cellular biology · 2006Article
- Proteomic analysis of interchromatin granule clusters.Molecular biology of the cell · 2004Article
- Transcriptional stimulation by the DNA binding protein Hap46/BAG-1M involves hsp70/hsc70 molecular chaperones.Nucleic acids research · 2003Article
- Par4 is a coactivator for a splice isoform-specific transcriptional activation domain in WT1.Genes & development · 2001Article
- The possible role and application of WT1 in human leukemia.International journal of hematology · 2001Review
- The chaperone function of hsp70 is required for protection against stress-induced apoptosis.Molecular and cellular biology · 2000Article
- Regulation of the Wilms' tumour suppressor protein transcriptional activation domain.Oncogene · 1999Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors at 4 institutions in 1 country.
Funding
Abstract
The Wilms tumor suppressor WT1 encodes a zinc finger transcription factor that is expressed in glomerular podocytes during a narrow window in kidney development. By immunoprecipitation and protein microsequencing analysis, we have identified a major cellular protein associated with endogenous WT1 to be the inducible chaperone Hsp70. WT1 and Hsp70 are physically associated in embryonic rat kidney cells, in primary Wilms tumor specimens and in cultured cells with inducible expression of WT1. Colocalization of WT1 and Hsp70 is evident within podocytes of the developing kidney, and Hsp70 is recruited to the characteristic subnuclear clusters that contain WT1. The amino-terminal transactivation domain of WT1 is required for binding to Hsp70, and expression of that domain itself is sufficient to induce expression of Hsp70 through the heat shock element (HSE). Substitution of a heterologous Hsp70-binding domain derived from human DNAJ is sufficient to restore the functional properties of a WT1 protein with an amino-terminal deletion, an effect that is abrogated by a point mutation in DNAJ that reduces binding to Hsp70. These observations indicate that Hsp70 is an important cofactor for the function of WT1, and suggest a potential role for this chaperone during kidney differentiation.
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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.