ArticleCell death & disease2012
High-mobility group A1 protein inhibits p53-mediated intrinsic apoptosis by interacting with Bcl-2 at mitochondria.
Article in Cell death & disease, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 21 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
21 citing papers in PubMed, 27 citations in OpenAlex.
- Article
- Transcriptomic and proteomic profiling reveal immune and metabolic dysregulation in the colonic mucosa of people living with HIV with incomplete immune recovery.Frontiers in immunology · 2025Article
- High Mobility Group A1 (HMGA1): Structure, Biological Function, and Therapeutic Potential.International journal of biological sciences · 2022Review
- Prognostic significance of high mobility group A2 (HMGA2) in pancreatic ductal adenocarcinoma: malignant functions of cytoplasmic HMGA2 expression.Journal of cancer research and clinical oncology · 2021Article
- STAT3 plays an important role in DNA replication by turning on WDHD1.Cell & bioscience · 2021Article
- HMGA1 exacerbates tumor growth through regulating the cell cycle and accelerates migration/invasion via targeting miR-221/222 in cervical cancer.Cell death & disease · 2018Article
- Rearrangement of mitochondrial pyruvate dehydrogenase subunit dihydrolipoamide dehydrogenase protein-protein interactions by the MDM2 ligand nutlin-3.Proteomics · 2016Article
- p53 and mitochondrial dysfunction: novel insight of neurodegenerative diseases.Journal of bioenergetics and biomembranes · 2016Review
- Association of SIRT1 and HMGA1 expression in non-small cell lung cancer.Oncology letters · 2016Article
- Disruptive environmental chemicals and cellular mechanisms that confer resistance to cell death.Carcinogenesis · 2015Review
- TAp73 promotes anabolism.Oncotarget · 2014Article
- HMGB1 in health and disease.Molecular aspects of medicine · 2014Review
- Article
- The PTTG1-binding factor (PBF/PTTG1IP) regulates p53 activity in thyroid cells.Endocrinology · 2014Article
- Inferring protein modulation from gene expression data using conditional mutual information.PloS one · 2014Article
- HMGA proteins as modulators of chromatin structure during transcriptional activation.Frontiers in cell and developmental biology · 2014Review
- Metabolic profiling of human CD4+ cells following treatment with methotrexate and anti-TNF-α infliximab.Cell cycle (Georgetown, Tex.) · 2013Article
- Molecular dynamics of the full-length p53 monomer.Cell cycle (Georgetown, Tex.) · 2013Article
- Caspase-1 is a novel target of p63 in tumor suppression.Cell death & disease · 2013Article
- Tamoxifen magnifies therapeutic impact of ceramide in human colorectal cancer cells independent of p53.Biochemical pharmacology · 2013Article
Corrections and comments
- Retraction · 2014-05-01Concerns/Issues about Image · Criminal Proceedings · Duplication of/in Image · Investigation by Company/Institution · Investigation by Third Party · Objections by Third Party ·
- Retracted
Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The high-mobility group A (HMGA) proteins are a family of non-histone chromatin factors, encoded by the HMGA1 and HMGA2 genes. Several studies demonstrate that HMGA proteins have a critical role in neoplastic transformation, and their overexpression is mainly associated with a highly malignant phenotype, also representing a poor prognostic index. Even though a cytoplasmic localization of these proteins has been previously reported in some highly malignant neoplasias, a clear role for this localization has not been defined. Here, we first confirm the localization of the HMGA1 proteins in the cytoplasm of cancer cells, and then we report a novel mechanism through which HMGA1 inhibits p53-mitochondrial apoptosis by counteracting the binding of p53 to the anti-apoptotic factor Bcl-2. Indeed, we demonstrate a physical and functional interaction between HMGA1 and Bcl-2 proteins. This interaction occurs at mitochondria interfering with the ability of p53 protein to bind Bcl-2, thus counteracting p53-mediated mitochondrial apoptosis. This effect is associated with the inhibition of cytochrome c release and activation of caspases. Consistent with this mechanism, a strong correlation between HMGA1 cytoplasmic localization and a more aggressive histotype of thyroid, breast and colon carcinomas has been observed. Therefore, cytoplasmic localization of HMGA1 proteins in malignant tissues is a novel mechanism of inactivation of p53 apoptotic function.
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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.