ArticleMolecular and cellular biology2002
Identification and characterization of a tissue-specific coactivator, GT198, that interacts with the DNA-binding domains of nuclear receptors.
Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 85 citations in OpenAlex.
- The Hop2-Mnd1 Complex and Its Regulation of Homologous Recombination.Biomolecules · 2023Review
- Decoding cancer and herbal renaissance.Longhua Chinese medicine · 2022Article
- Biallelic mutations in PSMC3IP are associated with secondary amenorrhea: expanding the spectrum of premature ovarian insufficiency.Journal of assisted reproduction and genetics · 2022Article
- Hop2 interacts with the transcription factor CEBPα and suppresses adipocyte differentiation.The Journal of biological chemistry · 2021Article
- Beyond the Double-Strand Breaks: The Role of DNA Repair Proteins in Cancer Stem-Cell Regulation.Cancers · 2021Review
- Shared genetics between nonobstructive azoospermia and primary ovarian insufficiency.F&S reviews · 2021Article
- GT198 Is a Target of Oncology Drugs and Anticancer Herbs.Frontiers in oral health · 2021Article
- Sign-based Shrinkage Based on an Asymmetric LASSO Penalty.Journal of data science : JDS · 2021Article
- Two auxiliary factors promote Dmc1-driven DNA strand exchange via stepwise mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Oncoprotein GT198 vaccination delays tumor growth in MMTV-PyMT mice.Cancer letters · 2020Article
- Hop2 Interacts with ATF4 to Promote Osteoblast Differentiation.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2019Article
- Primary Ovarian Insufficiency and Azoospermia in Carriers of a Homozygous PSMC3IP Stop Gain Mutation.The Journal of clinical endocrinology and metabolism · 2018Article
- An Approach to Greater Specificity for Glucocorticoids.Frontiers in endocrinology · 2018Review
- Malignant pericytes expressing GT198 give rise to tumor cells through angiogenesis.Oncotarget · 2017Article
- Article
- GT198 Expression Defines Mutant Tumor Stroma in Human Breast Cancer.The American journal of pathology · 2016Article
- Significance of ligand interactions involving Hop2-Mnd1 and the RAD51 and DMC1 recombinases in homologous DNA repair and XX ovarian dysgenesis.Nucleic acids research · 2015Article
- RXR agonist modulates TR: corepressor dissociation upon 9-cis retinoic acid treatment.Molecular endocrinology (Baltimore, Md.) · 2015Article
- Article
- Human ovarian cancer stroma contains luteinized theca cells harboring tumor suppressor gene GT198 mutations.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Gene activation mediated by nuclear receptors is regulated in a tissue-specific manner and requires interactions between nuclear receptors and their cofactors. Here, we identified and characterized a tissue-specific coactivator, GT198, that interacts with the DNA-binding domains of nuclear receptors. GT198 was originally described as a genomic transcript that mapped to the human breast cancer susceptibility locus 17q12-q21 with unknown function. We show that GT198 exhibits a tissue-specific expression pattern in which its mRNA is elevated in testis, spleen, thymus, pituitary cells, and several cancer cell lines. GT198 is a 217-amino-acid nuclear protein that contains a leucine zipper required for its dimerization. In vitro binding and yeast two-hybrid assays indicated that GT198 interacted with nuclear receptors through their DNA-binding domains. GT198 potently stimulated transcription mediated by estrogen receptor alpha and beta, thyroid hormone receptor beta1, androgen receptor, glucocorticoid receptor, and progesterone receptor. However, the action of GT198 was distinguishable from that of the ligand-binding domain-interacting nuclear receptor coactivators, such as TRBP, CBP, and SRC-1, with respect to basal activation and hormone sensitivity. Furthermore, protein kinase A, protein kinase C, and mitogen-activated protein kinase can phosphorylate GT198 in vitro, and cotransfection of these kinases regulated the transcriptional activity of GT198. These data suggest that GT198 is a tissue-specific, kinase-regulated nuclear receptor coactivator that interacts with the DNA-binding domains of nuclear receptors.
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