ArticleCell discovery2016
A novel role for the tumour suppressor Nitrilase1 modulating the Wnt/β-catenin signalling pathway.
Article in Cell discovery, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 19 citations in OpenAlex.
- WNT3a Signaling Inhibits Aromatase Expression in Breast Adipose Fibroblasts-A Possible Mechanism Supporting the Loss of Estrogen Responsiveness of Triple-Negative Breast Cancers.International journal of molecular sciences · 2023Article
- The Rosetta Stone Hypothesis-Based Interaction of the Tumor Suppressor Proteins Nit1 and Fhit.Cells · 2023Article
- Hyperforin and Myrtucommulone Derivatives Act as Natural Modulators of Wnt/β-Catenin Signaling in HCT116 Colon Cancer Cells.International journal of molecular sciences · 2022Article
- Characterization of the Nit6803 nitrilase homolog from the cyanotrophBiochemistry and biophysics reports · 2021Article
- Familial deep cavitating state with a glutathione metabolism defect.Annals of clinical and translational neurology · 2019Article
- Wnt Glycation Inhibits Canonical Signaling.Cells · 2019Article
- Apoptotic Fragmentation of Tricellulin.International journal of molecular sciences · 2019Article
- Gefitinib suppresses cervical cancer progression by inhibiting cell cycle progression and epithelial-mesenchymal transition.Experimental and therapeutic medicine · 2019Article
- Activation of the ERK/Creb/Bcl‑2 pathway protects periodontal ligament stem cells against hydrogen peroxide‑induced oxidative stress.Molecular medicine reports · 2019Article
- Using Drosophila Models and Tools to Understand the Mechanisms of Novel Human Cancer Driver Gene Function.Advances in experimental medicine and biology · 2019Review
- Nit1 is a metabolite repair enzyme that hydrolyzes deaminated glutathione.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- SUMOylation regulates the intracellular fate of ZO-2.Cellular and molecular life sciences : CMLS · 2017Article
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nitrilase1 was classified as a tumour suppressor in association with the fragile histidine-triad protein Fhit. However, knowledge about nitrilase1 and its tumour suppressor function is still limited. Whereas nitrilase1 and Fhit are discrete proteins in mammals, they are merged in Drosophila melanogaster and Caenorhabditis elegans. According to the Rosetta-Stone hypothesis, proteins encoded as fusion proteins in one organism and as separate proteins in another organism may act in the same signalling pathway. Although a direct interaction of human nitrilase1 and Fhit has not been shown, our previous finding that Fhit interacts with β-catenin and represses its transcriptional activity in the canonical Wnt pathway suggested that human nitrilase1 also modulates Wnt signalling. In fact, human nitrilase1 forms a complex with β-catenin and LEF-1/TCF-4, represses β-catenin-mediated transcription and shows an additive effect together with Fhit. Knockdown of human nitrilase1 enhances Wnt target gene expression. Moreover, our experiments show that β-catenin competes away human nitrilase1 from LEF-1/TCF and thereby contributes to the activation of Wnt-target gene transcription. Inhibitory activity of human nitrilase1 on vertebrate Wnt signalling was confirmed by repression of Wnt-induced double axis formation in Xenopus embryogenesis. In line with this finding, the Drosophila fusion protein Drosophila NitFhit directly binds to Armadillo and represses the Wingless pathway in reporter gene assays. Genetic experiments confirmed the repressive activity of Drosophila NitFhit on Wingless signalling in the Drosophila wing imaginal disc. In addition, colorectal tumour microarray analysis revealed a significantly reduced expression of human nitrilase1 in poorly differentiated tumours. Taken together, repression of the canonical Wnt pathway represents a new mechanism for the human nitrilase1 tumour suppressor function.
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