ArticleThe EMBO journal1999
The interferon-inducible nucleolar p204 protein binds the ribosomal RNA-specific UBF1 transcription factor and inhibits ribosomal RNA transcription.
Article in The EMBO journal, 1999. 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, 74 citations in OpenAlex.
- Structural mechanism of DNA recognition by the p204 HIN domain.Nucleic acids research · 2021Article
- Activation and Immune Regulation Mechanisms of PYHIN Family During Microbial Infection.Frontiers in microbiology · 2021Review
- Ifi204/p204, a new piece in the sepsis puzzle.Annals of translational medicine · 2018Article
- RNA-Seq analysis of interferon inducible p204-mediated network in anti-tumor immunity.Scientific reports · 2018Article
- p204 Is Required for Canonical Lipopolysaccharide-induced TLR4 Signaling in Mice.EBioMedicine · 2018Article
- The roles of interferon-inducible p200 family members IFI16 and p204 in innate immune responses, cell differentiation and proliferation.Genes & diseases · 2015Article
- Wanderings in biochemistry.The Journal of biological chemistry · 2014Article
- IFN-α-driven CCL2 production recruits inflammatory monocytes to infection site in mice.Mucosal immunology · 2013Article
- Resistance to HSV-1 infection in the epithelium resides with the novel innate sensor, IFI-16.Mucosal immunology · 2012Article
- IFI16 is an innate immune sensor for intracellular DNA.Nature immunology · 2010Article
- Interaction between cartilage oligomeric matrix protein and extracellular matrix protein 1 mediates endochondral bone growth.Matrix biology : journal of the International Society for Matrix Biology · 2010Article
- The p200 family protein p204 as a modulator of cell proliferation and differentiation: a brief survey.Cellular and molecular life sciences : CMLS · 2010Review
- p204 protein overcomes the inhibition of core binding factor alpha-1-mediated osteogenic differentiation by Id helix-loop-helix proteins.Molecular biology of the cell · 2008Article
- ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein.The Journal of biological chemistry · 2006Article
- ADAMTS-7: a metalloproteinase that directly binds to and degrades cartilage oligomeric matrix protein.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2006Article
- Control of cell size through phosphorylation of upstream binding factor 1 by nuclear phosphatidylinositol 3-kinase.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Calmodulin binds to the C terminus of sodium channels Nav1.4 and Nav1.6 and differentially modulates their functional properties.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2003Article
- The cell death regulator GRIM-19 is an inhibitor of signal transducer and activator of transcription 3.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Expression of IFI 16 in epithelial cells and lymphoid tissues.Histochemistry and cell biology · 2003Article
- The MyoD-inducible p204 protein overcomes the inhibition of myoblast differentiation by Id proteins.Molecular and cellular biology · 2002Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
p204, a member of the interferon-inducible p200 family of murine proteins, is primarily nucleolar. We generated cell lines in which p204 was inducible by muristerone. This induction resulted in retardation of cell proliferation and inhibition of rRNA transcription in vivo. Interferon treatment, resulting in p204 induction and retardation of proliferation, also caused inhibition of rRNA transcription in vivo. p204 also inhibited rRNA transcription in vitro. This inhibition was overcome by addition of UBF1, the rRNA-specific transcription factor. A direct interaction between p204 and UBF1 was revealed in vitro in pull-down assays, and in vivo by co-immunoprecipitation from cell extracts. UBF1 bound strongly to at least two regions of p204: the N-terminal segment linked to the conserved 200 amino acid a segment, and the conserved 200 amino acid b segment. Cleavage of the a or b segments into two segments (encoded by single exons) resulted in a strong decrease or loss of binding. The inhibition of rRNA transcription by p204 may be due to the inhibition by p204 of the specific DNA binding of UBF1. This was revealed in electrophoretic mobility shift, magnetic bead and footprinting assays. Thus, p204 serves as a mediator of the inhibition of rRNA transcription by interferon.
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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.