Relevant bibliographies by topics / BRCA1/BARD1 interactions

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Academic literature on the topic 'BRCA1/BARD1 interactions'

Author: Grafiati
Published: 4 June 2021
Last updated: 8 February 2022

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Journal articles on the topic "BRCA1/BARD1 interactions"

1

Watters, Andrea K., Emily S. Seltzer, Danny MacKenzie, Melody Young, Jonathan Muratori, Rama Hussein, Andrej M. Sodoma, Julie To, Manrose Singh, and Dong Zhang. "The Effects of Genetic and Epigenetic Alterations of BARD1 on the Development of Non-Breast and Non-Gynecological Cancers." Genes 11, no. 7 (July 21, 2020): 829. http://dx.doi.org/10.3390/genes11070829.

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Breast Cancer 1 (BRCA1) gene is a well-characterized tumor suppressor gene, mutations of which are primarily found in women with breast and ovarian cancers. BRCA1-associated RING domain 1 (BARD1) gene has also been identified as an important tumor suppressor gene in breast, ovarian, and uterine cancers. Underscoring the functional significance of the BRCA1 and BARD1 interactions, prevalent mutations in the BRCA1 gene are found in its RING domain, through which it binds the RING domain of BARD1. BARD1-BRCA1 heterodimer plays a crucial role in a variety of DNA damage response (DDR) pathways, including DNA damage checkpoint and homologous recombination (HR). However, many mutations in both BARD1 and BRCA1 also exist in other domains that significantly affect their biological functions. Intriguingly, recent genome-wide studies have identified various single nucleotide polymorphisms (SNPs), genetic alterations, and epigenetic modifications in or near the BARD1 gene that manifested profound effects on tumorigenesis in a variety of non-breast and non-gynecological cancers. In this review, we will briefly discuss the molecular functions of BARD1, including its BRCA1-dependent as well as BRCA1-independent functions. We will then focus on evaluating the common BARD1 related SNPs as well as genetic and epigenetic changes that occur in the non-BRCA1-dominant cancers, including neuroblastoma, lung, and gastrointestinal cancers. Furthermore, the pro- and anti-tumorigenic functions of different SNPs and BARD1 variants will also be discussed.
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Caleca, Laura, Mara Colombo, Thomas van Overeem Hansen, Conxi Lázaro, Siranoush Manoukian, Michael T. Parsons, Amanda B. Spurdle, and Paolo Radice. "GFP-Fragment Reassembly Screens for the Functional Characterization of Variants of Uncertain Significance in Protein Interaction Domains of the BRCA1 and BRCA2 Genes." Cancers 11, no. 2 (January 28, 2019): 151. http://dx.doi.org/10.3390/cancers11020151.

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Genetic testing for BRCA1 and BRCA2 genes has led to the identification of many unique variants of uncertain significance (VUS). Multifactorial likelihood models that predict the odds ratio for VUS in favor or against cancer causality, have been developed, but their use is conditioned by the amount of necessary data, which are difficult to obtain if a variant is rare. As an alternative, variants mapping to the coding regions can be examined using in vitro functional assays. BRCA1 and BRCA2 proteins promote genome protection by interacting with different proteins. In this study, we assessed the functional effect of two sets of variants in BRCA genes by exploiting the green fluorescent protein (GFP)-reassembly in vitro assay, which was set-up to test the BRCA1/BARD1, BRCA1/UbcH5a, and BRCA2/DSS1 interactions. Based on the findings observed for the validation panels of previously classified variants, BRCA1/UbcH5a and BRCA2/DSS1 binding assays showed 100% sensitivity and specificity in identifying pathogenic and non-pathogenic variants. While the actual efficiency of these assays in assessing the clinical significance of BRCA VUS has to be verified using larger validation panels, our results suggest that the GFP-reassembly assay is a robust method to identify variants affecting normal protein functioning and contributes to the classification of VUS.
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Morris, Joanna R. "Is it a wrap? Nucleosome interactions of the BRCA1-binding partner, BARD1, steal the scene." Nature Structural & Molecular Biology 28, no. 9 (September 2021): 708–10. http://dx.doi.org/10.1038/s41594-021-00658-7.

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Sarkar, Mohosin, and Thomas J. Magliery. "Re-engineering a split-GFP reassembly screen to examine RING-domain interactions between BARD1 and BRCA1 mutants observed in cancer patients." Molecular BioSystems 4, no. 6 (2008): 599. http://dx.doi.org/10.1039/b802481b.

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McCarthy, Ellen E., Julide T. Celebi, Richard Baer, and Thomas Ludwig. "Loss of Bard1, the Heterodimeric Partner of the Brca1 Tumor Suppressor, Results in Early Embryonic Lethality and Chromosomal Instability." Molecular and Cellular Biology 23, no. 14 (July 15, 2003): 5056–63. http://dx.doi.org/10.1128/mcb.23.14.5056-5063.2003.

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ABSTRACT The BRCA1 tumor suppressor has been implicated in many cellular pathways, but the mechanisms by which it suppresses tumor formation are not fully understood. In vivo BRCA1 forms a heterodimeric complex with the related BARD1 protein, and its enzymatic activity as a ubiquitin ligase is largely dependent upon its interaction with BARD1. To explore the genetic relationship between BRCA1 and BARD1, we have examined the phenotype of Bard1-null mice. These mice become developmentally retarded and die between embryonic day 7.5 (E7.5) and E8.5. Embryonic lethality results from a severe impairment of cell proliferation that is not accompanied by increased apoptosis. In the absence of p53, the developmental defects associated with Bard1 deficiency are partly ameliorated, and the lethality of Bard1; p53-nullizygous mice is delayed until E9.5. This result, together with the increased chromosomal aneuploidy of Bard1 mutant cells, indicates a role for Bard1 in maintaining genomic stability. The striking similarities between the phenotypes of Bard1-null, Brca1-null, and double Bard1; Brca1-null mice provide strong genetic evidence that the developmental functions of Brca1 and Bard1 are mediated by the Brca1/Bard1 heterodimer.
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Wu-Baer, Foon, Thomas Ludwig, and Richard Baer. "The UBXN1 Protein Associates with Autoubiquitinated Forms of the BRCA1 Tumor Suppressor and Inhibits Its Enzymatic Function." Molecular and Cellular Biology 30, no. 11 (March 29, 2010): 2787–98. http://dx.doi.org/10.1128/mcb.01056-09.

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ABSTRACT Although the BRCA1 tumor suppressor has been implicated in many cellular processes, the biochemical mechanisms by which it influences these diverse pathways are poorly understood. The only known enzymatic function of BRCA1 is the E3 ubiquitin ligase activity mediated by its highly conserved RING domain. In vivo, BRCA1 associates with the BARD1 polypeptide to form a heterodimeric BRCA1/BARD1 complex that catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. In most cases, BRCA1-dependent ubiquitination generates polyubiquitin chains bearing an unconventional K6 linkage that does not appear to target proteins for proteasomal degradation. Since ubiquitin-dependent processes are usually mediated by cellular receptors with ubiquitin-binding motifs, we screened for proteins that specifically bind autoubiquitinated BRCA1. Here we report that the UBXN1 polypeptide, which contains a ubiquitin-associated (UBA) motif, recognizes autoubiquitinated BRCA1. This occurs through a bipartite interaction in which the UBA domain of UBXN1 binds K6-linked polyubiquitin chains conjugated to BRCA1 while the C-terminal sequences of UBXN1 bind the BRCA1/BARD1 heterodimer in a ubiquitin-independent fashion. Significantly, the E3 ligase activity of BRCA1/BARD1 is dramatically reduced in the presence of UBXN1, suggesting that UBXN1 regulates the enzymatic function of BRCA1 in a manner that is dependent on its ubiquitination status.
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Kim, Kang Ho, Jeong Min Yoon, A. Hyun Choi, Woo Sik Kim, Gha Young Lee, and Jae Bum Kim. "Liver X Receptor Ligands Suppress Ubiquitination and Degradation of LXRα by Displacing BARD1/BRCA1." Molecular Endocrinology 23, no. 4 (April 1, 2009): 466–74. http://dx.doi.org/10.1210/me.2008-0295.

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Abstract Liver X receptor (LXR) is a ligand-activated transcription factor that plays important roles in cholesterol and lipid homeostasis. However, ligand-induced posttranslational modification of LXR is largely unknown. Here, we show that ligand-free LXRα is rapidly degraded by ubiquitination. Without ligand, LXRα interacts with an ubiquitin E3-ligase protein complex containing breast and ovarian cancer susceptibility 1 (BRCA1)-associated RING domain 1 (BARD1). Interestingly, LXR ligand represses ubiquitination and degradation of LXRα, and the interaction between LXRα and BARD1 is inhibited by LXR ligand. Consistently, T0901317, a synthetic LXR ligand, increased the level of LXRα protein in liver. Moreover, overexpression of BARD1/BRCA1 promoted the ubiquitination of LXRα and reduced the recruitment of LXRα to the target gene promoters, whereas BARD1 knockdown reversed such effects. Taken together, these data suggest that LXR ligand prevents LXRα from ubiquitination and degradation by detaching BARD1/BRCA1, which might be critical for the early step of transcriptional activation of ligand-stimulated LXRα through a stable binding of LXRα to the promoters of target genes.
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Tambaro, Francesco Paolo, Ilaria Lepore, Carmela Dell Aversana, Floriana De Bellis, Marco Miceli, Vincenzo Carafa, Angela Nebbioso, Felicetto Ferrara, Guillermo garcia Manero, and Lucia Altucci. "BARD1: a New Target In Leukemia." Blood 116, no. 21 (November 19, 2010): 4642. http://dx.doi.org/10.1182/blood.v116.21.4642.4642.

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Abstract Abstract 4642 Background BARD1 (BRCA1-associated RING domain protein 1) was first described as a BRCA1 partner and tumour suppressor protein, muted in most cases of breast and ovarian cancer. BARD1 functions are BRCA1-dependent, requiring formation of a stable heterodimer through interaction of the RING finger domains. BRCA1-independent functions for BARD1 have recently been described, making it an interesting and important molecule for study. BARD1 is expressed in almost all human tissues, including haematological cells, testis and breast tissue, but it is over-expressed in leukaemias, sarcomas and testis cancer, implicating BARD1 in development of cancer. Different BARD1 isoforms are up-regulated in breast, ovarian and uterine cancers but markedly down-regulated or absent in healthy tissues. Therefore, the presence of these isoforms might be a risk factor or causal event in the cancer pathogenesis. We investigated the role of BARD1 isoforms in leukaemia, through the study of the epigenetic mechanisms involved in regulation of its expression and function. As such, we determined the expression of a specific BARD1 isoform in different human leukaemia cell lines the effects of the histone deacetylase inhibitor SAHA (suberoylanilide hydroxamic acid, Vorinostat) of expression of BARD1. Results. Four human leukaemia cell lines (U937, NB4, K562 and HL60) express the BARD1 isoform of interest. Treatment of these cell lines with SAHA at 5 μ M resulted in decreased expression of this isoform (Fig. 1). Decreased expression of BARD1 by SAHA was also observed in in human breast cancer MCF7 cells, the usual model for BARD1 experiments and in the human neuroblastoma cell line Kelly (Fig. 2), but not in HeLa cells or an human epithelial carcinoma cell line (Fig. 2). The reduced expression of BARD1 was attributed to the action of 2 specific micro-RNAs (miRNAs), that directly bind its 3′untranslated region (UTR). SAHA-induced expression of miR-19a and miR-19b in primary human leukemia cells as demonstrated using miRNA microarray expression analysis and confirmed by Real-Time PCR (Fig. 3). These 2 miRNA were up-regulated after SAHA stimulation in human leukaemia cells. BARD1 is the predicted target for miR-19a and miR-19b based on miRBase database analyses. Transient transfection in NB4 cells with mimic miR-19a and mimic miR-19b confirmed expression of these miRNAs was associated with BARD1 down-regulation (Fig. 4 5.). The BARD1 3′UTR was cloned into a pGL3 vector with a downstream the luciferase gene reporting gene (Fig. 6). The plasmid was co-transfected in HeLa cells with each mimic miRNA and a luciferase assay was performed. We demonstrate that expression of miR-19a and miR-19b can directly bind BARD1 3′UTR, reducing luciferase activity in this system (Fig. 7), thereby confirming that BARD1 is a target of these miRNAs. These findings support our hypothesis that BARD1 is a promising target in leukemia and should be further investigated for its diagnostic and prognostic features. Disclosures: No relevant conflicts of interest to declare.
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9

Sharma, Amit, Arijit Biswas, Hongde Liu, Sagnik Sen, Anoosha Paruchuri, Panagiotis Katsonis, Olivier Lichtarge, et al. "Mutational Landscape of the BAP1 Locus Reveals an Intrinsic Control to Regulate the miRNA Network and the Binding of Protein Complexes in Uveal Melanoma." Cancers 11, no. 10 (October 19, 2019): 1600. http://dx.doi.org/10.3390/cancers11101600.

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The BAP1 (BRCA1-associated protein 1) gene is associated with a variety of human cancers. With its gene product being a nuclear ubiquitin carboxy-terminal hydrolase with deubiquitinase activity, BAP1 acts as a tumor suppressor gene with potential pleiotropic effects in multiple tumor types. Herein, we focused specifically on uveal melanoma (UM) in which BAP1 mutations are associated with a metastasizing phenotype and decreased survival rates. We identified the ubiquitin carboxyl hydrolase (UCH) domain as a major hotspot region for the pathogenic mutations with a high evolutionary action (EA) score. This also includes the mutations at conserved catalytic sites and the ones overlapping with the phosphorylation residues. Computational protein interaction studies revealed that distant BAP1-associated protein complexes (FOXK2, ASXL1, BARD1, BRCA1) could be directly impacted by this mutation paradigm. We also described the conformational transition related to BAP1-BRCA-BARD1 complex, which may pose critical implications for mutations, especially at the docking interfaces of these three proteins. The mutations affect - independent of being somatic or germline - the binding affinity of miRNAs embedded within the BAP1 locus, thereby altering the unique regulatory network. Apart from UM, BAP1 gene expression and survival associations were found to be predictive for the prognosis in several (n = 29) other cancer types. Herein, we suggest that although BAP1 is conceptually a driver gene in UM, it might contribute through its interaction partners and its regulatory miRNA network to various aspects of cancer. Taken together, these findings will pave the way to evaluate BAP1 in a variety of other human cancers with a shared mutational spectrum.
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10

Chen, Yong-Zi, Duo Zuo, Hai-Ling Ren, Sai-Jun Fan, and Guoguang Ying. "Bioinformatics Analysis of Expression and Alterations of BARD1 in Breast Cancer." Technology in Cancer Research & Treatment 18 (January 1, 2019): 153303381989226. http://dx.doi.org/10.1177/1533033819892260.

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Background: Breast cancer is one of the most common malignant tumor type in women worldwide. BARD1 could impact function of BRCA1 as its interaction partner. In the current study, we aimed to investigate the prognostic role of BARD1 expression as well as its alterations in breast cancer using different online tools. Methods: We performed a bioinformatics analysis for BARD1 in patients with breast cancer using several online databases, including Oncomine, bc-GenExMiner, PrognoScan, Search Tool for the Retrieval of Interacting Genes, Cytoscape, and cBioPortal. Results: We found that BARD1 was highly expressed in basal-like, HER2-E, and luminal B compared with normal-like subtype. Forest plot showed that BARD1 overexpression was correlated with worse distant metastasis-free survival (hazard ratio: 2.72, 95% confidence interval: 1.02-2.21; P = .0448), disease-specific survival (hazard ratio: 2.65, 95% confidence interval: 1.37-5.12; P = .0037), and disease-free survival (hazard ratio: 1.98, 95% confidence interval: 1.22-3.24; P = .0062) but positively correlated with overall survival (hazard ratio: 0.66, 95% confidence interval: 0.50-0.85; P = .0017). Multivariate analysis indicated that BARD1 expression was significantly associated with distant metastasis-free survival (hazard ratio: 4.60, 95% confidence interval: 1.22-17.28; P = .0239) whereas marginally significant for disease-free survival (hazard ratio: 1.00, 95% confidence interval: 1.00-1.01, P = .0630) and disease-specific survival (hazard ratio: 1.96, 95% confidence interval: 0.97-3.96; P = .0602). Meanwhile, alterations in BARD1 interaction network were associated with worse overall survival instead of BARD1 alteration alone. Conclusions: Bioinformatics analysis revealed that BARD1 may be a predictive biomarker for prognosis of breast cancer. However, future research is required to validate our findings.
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Dissertations / Theses on the topic "BRCA1/BARD1 interactions"

1

Christensen, Devin Eugene. "Identifying substrate and E2 interactions of the BRCA1/BARD1 ubiquitin ligase /." Thesis, Connect to this title online; UW restricted, 2007. http://hdl.handle.net/1773/9222.

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Rice, Ian S. "Honors Thesis: BRCA1 Interactions with BACH1, BARD1, and CHK2: Recent Evidence and Potential Developments in the Diagnosis, Treatment, and Prevention of Human Breast Cancer." Miami University Honors Theses / OhioLINK, 2005. http://rave.ohiolink.edu/etdc/view?acc_num=muhonors1114185039.

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Sarkar, Mohosin M. "Engineering Proteins with GFP: Study of Protein-Protein Interactions In vivo, Protein Expression and Solubility." The Ohio State University, 2009. http://rave.ohiolink.edu/etdc/view?acc_num=osu1261418776.

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Conference papers on the topic "BRCA1/BARD1 interactions"

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Adamovich, Aleksandra, Margaret Wingo, Tapahsama Banerjee, Miranda Gardner, Michael Freitas, and Jeffrey Parvin. "Abstract 1367: BRCA1 and BARD1 protein interactions that are required for DNA repair function." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-1367.

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Nepomuceno, Thales C., Vanessa C. Fernandes, Giuliana D. Gregoris, Renato S. Carvalho, Álvaro N. Monteiro, and Marcelo A. Carvalho. "Abstract 480: CDK9 (a novel BRCA1/BARD1 interaction partner) downregulates BRCA1-mediated transcription." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-480.

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