ArticleOncogene2005
Structural determinants of the BRCA1 : estrogen receptor interaction.
Article in Oncogene, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 54 citations in OpenAlex.
- A New Class of BRCA1 Mimetics for ERα-Positive Breast Cancer Therapy: Design, Synthesis, In Silico Screening, In Vitro Assay, and Gene Expression Analysis.Life (Basel, Switzerland) · 2025Article
- BRCA1-mimetic compound NSC35446.HCl inhibits IKKB expression by reducing estrogen receptor-α occupancy in the IKKB promoter and inhibits NF-κB activity in antiestrogen-resistant human breast cancer cells.Breast cancer research and treatment · 2017Article
- SNPs near the cysteine proteinase cathepsin O gene (CTSO) determine tamoxifen sensitivity in ERα-positive breast cancer through regulation of BRCA1.PLoS genetics · 2017Article
- A new class of small molecule estrogen receptor-alpha antagonists that overcome anti-estrogen resistance.Oncotarget · 2015Article
- Risk factors for endometrial cancer among women with a BRCA1 or BRCA2 mutation: a case control study.Familial cancer · 2015Article
- Small-molecule "BRCA1-mimetics" are antagonists of estrogen receptor-α.Molecular endocrinology (Baltimore, Md.) · 2014Article
- Elevated estrogen receptor-α in VHL-deficient condition induces microtubule organizing center amplification via disruption of BRCA1/Rad51 interaction.Neoplasia (New York, N.Y.) · 2014Article
- Comparative analysis of human tissue interactomes reveals factors leading to tissue-specific manifestation of hereditary diseases.PLoS computational biology · 2014Article
- Derailed estrogen signaling and breast cancer: an authentic couple.Endocrine reviews · 2013Review
- Expression of estrogen-related gene markers in breast cancer tissue predicts aromatase inhibitor responsiveness.PloS one · 2013Article
- BRCA-1 and BRCA-2 mutation bedside detection and breast cancer clinical primary prevention.Frontiers in genetics · 2013Article
- Review
- Ligand-dependent differences in estrogen receptor beta-interacting proteins identified in lung adenocarcinoma cells corresponds to estrogenic responses.Proteome science · 2011Article
- Assessing estrogen signaling aberrations in breast cancer risk using genetically engineered mouse models.Annals of the New York Academy of Sciences · 2011Review
- Hakai acts as a coregulator of estrogen receptor alpha in breast cancer cells.Cancer science · 2010Article
- BRCA1 deficient mouse models to study pathogenesis and therapy of triple negative breast cancer.Breast disease · 2010Review
- BRCA1 regulates acetylation and ubiquitination of estrogen receptor-alpha.Molecular endocrinology (Baltimore, Md.) · 2010Article
- Mechanism of BRCA1-mediated inhibition of progesterone receptor transcriptional activity.Molecular endocrinology (Baltimore, Md.) · 2009Article
- A novel mechanism whereby BRCA1/1a/1b fine tunes the dynamic complex interplay between SUMO-dependent/independent activities of Ubc9 on E2-induced ERalpha activation/repression and degradation in breast cancer cells.International journal of oncology · 2009Article
- Decreased BRCA1 confers tamoxifen resistance in breast cancer cells by altering estrogen receptor-coregulator interactions.Oncogene · 2009Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Previously, we showed that the BRCA1 protein interacts directly and functionally with estrogen receptor-alpha (ER-alpha), resulting in the inhibition of estradiol (E2)-stimulated ER-alpha transcriptional activity. The interaction sites were mapped to the N-terminus of BRCA1 (within amino acids (aa) 1-302) and the ligand-binding domain/activation function-2 (LBD/AF-2) region (within aa 282-420) of ER-alpha. In this study, we have further characterized the structure/function relationship for the BRCA1 : ER-alpha interaction. We found that the N-terminal RING domain (aa 20-64) is not required for the BRCA1 : ER-alpha interaction. We identified two separate contact points for ER-alpha, one within aa 1-100 and the other within aa 100-200 of BRCA1; and we showed that each of these BRCA1 peptides interacts with BRCA1 in vitro and in vivo. By using different fragments of the BRCA1 N-terminus, we found that aa 67-100 and 101-133 are required for the interaction with ER-alpha, but that aa 1-67 and 134-302 are dispensible. Previously, we showed that BRCA1 aa 1-302 does not inhibit E2-stimulated ER-alpha transcriptional activity but does bind to ER-alpha and acts as a dominant negative inhibitor of the full-length BRCA1 protein. Somewhat surprisingly, we found that BRCA1 aa 1-100 and BRCA1 aa 101-200 (but not aa 201-300) each inhibited ER-alpha activity, although not as efficiently as full-length BRCA1. Mutations within an HIV Rev-like nuclear export signal that resembles a nuclear receptor corepressor motif (aa 86-95) impaired the ability of both truncated (aa 1-100) and full-length (aa 1-1863) BRCA1 proteins to interact with and/or repress ER-alpha activity. Based on these findings, a partial BRCA1 : ER-alpha three-dimensional structure is proposed. The implications of these findings for understanding the BRCA1 : ER-alpha interaction are discussed.
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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.