ArticleProceedings of the National Academy of Sciences of the United States of America1995
Functional antagonism between the retinoic acid receptor and the viral transactivator BZLF1 is mediated by protein-protein interactions.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 34 citations in OpenAlex.
- Cells Isolated from Regenerating Caudal Fin of Sparus aurata Can Differentiate into Distinct Bone Cell Lineages.Marine biotechnology (New York, N.Y.) · 2020Article
- RARα supports the development of Langerhans cells and langerin-expressing conventional dendritic cells.Nature communications · 2018Article
- Development of an in vitro cell system from zebrafish suitable to study bone cell differentiation and extracellular matrix mineralization.Zebrafish · 2013Article
- Development and characterization of Xl1, a Xenopus laevis chondrocyte-like cell culture.Molecular and cellular biochemistry · 2013Article
- Identification of retinoic acid as an inhibitor of transcription factor Nrf2 through activation of retinoic acid receptor alpha.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- The thyroid hormone receptor antagonizes CREB-mediated transcription.The EMBO journal · 2003Article
- X-ray structure of the orphan nuclear receptor RORbeta ligand-binding domain in the active conformation.The EMBO journal · 2001Article
- Modulation of CRX transactivation activity by phosducin isoforms.Molecular and cellular biology · 2000Article
- Differential ligand-dependent protein-protein interactions between nuclear receptors and a neuronal-specific cofactor.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Characterization of the DNA-binding and dimerization properties of the nuclear orphan receptor germ cell nuclear factor.Molecular and cellular biology · 1999Article
- The Epstein-Barr virus lytic transactivator Zta interacts with the helicase-primase replication proteins.Journal of virology · 1998Article
- The Epstein-Barr virus Rta protein activates lytic cycle genes and can disrupt latency in B lymphocytes.Journal of virology · 1998Article
- Physical interaction between retinoic acid receptor and the oncoprotein myb inhibits retinoic acid-dependent transactivation.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Identification of a novel negative retinoic acid responsive element in the promoter of the human matrix Gla protein gene.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- The transcriptional integrator CREB-binding protein mediates positive cross talk between nuclear hormone receptors and the hematopoietic bZip protein p45/NF-E2.Molecular and cellular biology · 1997Article
- The helix-loop-helix transcription factor SEF-2 regulates the activity of a novel initiator element in the promoter of the human somatostatin receptor II gene.The EMBO journal · 1996Article
- Functional analysis of retinoid Z receptor beta, a brain-specific nuclear orphan receptor.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Epstein-Barr virus-encoded protein BZLF1 is a member of the basic leucine zipper (bZip) family of transcription factors. Like several other members of the bZip family, transcriptional activity of BZLF1 is modulated by retinoic acid receptors (RARs). We present evidence that the RAR alpha and BZLF1 can reciprocally repress each other's transcriptional activation by a newly discovered mechanism. Analysis of RAR alpha mutants in transfection studies reveals that the DNA binding domain is sufficient for inhibition of BZLF1 activity. Analysis of BZLF1 mutants indicates that both the coiled-coil dimerization domain and a region containing the transcriptional activation domain of BZLF1 are required for transrepression. Coimmunoprecipitation experiments demonstrate physical interactions between RAR alpha and BZLF1 in vivo. Furthermore, glutathione S-transferase-pulldown assays reveal that these protein-protein interactions are mediated by the coiled-coil dimerization domain of BZLF1 and the DNA binding domain of RAR alpha. While RAR alpha is unable to recognize BZLF1 binding sites, the RAR alpha can be tethered to the DNA by forming a heteromeric complex with BZLF1 bound to DNA. Tethering RARs via protein-protein interactions onto promoter DNA suggest a mechanism through which RARs might gain additional levels of transcriptional regulation.
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