ArticleInternational journal of oncology2012
Targeting cysteine-mediated dimerization of the MUC1-C oncoprotein in human cancer cells.
Article in International journal of oncology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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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
58 citing papers in PubMed, 71 citations in OpenAlex.
- Evolution of the MUC1 gene in eutherian mammals as an adaptation responsible for the increasing incidence of cancer in humans.Biochimica et biophysica acta. Reviews on cancer · 2026Review
- MUCIN 1 confers inflammatory memory of tyrosine kinase inhibitor resistance in non-small cell lung cancer.Signal transduction and targeted therapy · 2025Article
- Research progress of MUC1 in genitourinary cancers.Cellular & molecular biology letters · 2024Review
- Emergence ofCancers · 2022Review
- Dependence on the MUC1-C Oncoprotein in Classic, Variant, and Non-neuroendocrine Small Cell Lung Cancer.Molecular cancer research : MCR · 2022Article
- MUC1 is a potential target to overcome trastuzumab resistance in breast cancer therapy.Cancer cell international · 2022Review
- MUC1-C dictates neuroendocrine lineage specification in pancreatic ductal adenocarcinomas.Carcinogenesis · 2022Article
- Chronic activation of MUC1-C in wound repair promotes progression to cancer stem cells.Journal of cancer metastasis and treatment · 2022Article
- MUC1 is an oncoprotein with a significant role in apoptosis (Review).International journal of oncology · 2021Review
- Mucins reprogram stemness, metabolism and promote chemoresistance during cancer progression.Cancer metastasis reviews · 2021Review
- MUC1-C Activates the BAF (mSWI/SNF) Complex in Prostate Cancer Stem Cells.Cancer research · 2021Article
- Targeting MUC1-C reverses the cisplatin resistance of esophageal squamous cell carcinomaTranslational cancer research · 2021Article
- MUC1-C in chronic inflammation and carcinogenesis; emergence as a target for cancer treatment.Carcinogenesis · 2020Review
- Comprehensive analysis of the mechanism and treatment significance of Mucins in lung cancer.Journal of experimental & clinical cancer research : CR · 2020Review
- MUC1-C drives stemness in progression of colitis to colorectal cancer.JCI insight · 2020Article
- MUC1-C regulates lineage plasticity driving progression to neuroendocrine prostate cancer.Nature communications · 2020Article
- Targeting MUC1-C Inhibits TWIST1 Signaling in Triple-Negative Breast Cancer.Molecular cancer therapeutics · 2019Article
- Inhibition of MUC1-C regulates metabolism by AKT pathway in esophageal squamous cell carcinoma.Journal of cellular physiology · 2019Article
- ACPred: A Computational Tool for the Prediction and Analysis of Anticancer Peptides.Molecules (Basel, Switzerland) · 2019Article
- MUC1-C Integrates Chromatin Remodeling and PARP1 Activity in the DNA Damage Response of Triple-Negative Breast Cancer Cells.Cancer research · 2019Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The MUC1 heterodimeric protein is aberrantly overexpressed in diverse human carcinomas and contributes to the malignant phenotype. The MUC1-C transmembrane subunit contains a CQC motif in the cytoplasmic domain that has been implicated in the formation of dimers and in its oncogenic function. The present study demonstrates that MUC1-C forms dimers in human breast and lung cancer cells. MUC1-C dimerization was detectable in the cytoplasm and was independent of MUC1-N, the N-terminal mucin subunit that extends outside the cell. We show that the MUC1-C cytoplasmic domain forms dimers in vitro that are disrupted by reducing agents. Moreover, dimerization of the MUC1-C subunit in cancer cells was blocked by reducing agents and increased by oxidative stress, supporting involvement of the CQC motif in forming disulfide bonds. In support of these observations, mutation of the MUC1-C CQC motif to AQA completely blocked MUC1-C dimerization. Importantly, this study was performed with MUC1-C devoid of fluorescent proteins, such as GFP, CFP and YFP. In this regard, we show that GFP, CFP and YFP themselves form dimers that are readily detectable with cross-linking agents. The present results further demonstrate that a cell-penetrating peptide that targets the MUC1-C CQC cysteines blocks MUC1-C dimerization in cancer cells. These findings provide definitive evidence that: i) the MUC1-C cytoplasmic domain cysteines are necessary and sufficient for MUC1-C dimerization, and ii) these CQC motif cysteines represent an Achilles' heel for targeting MUC1-C function.
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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.