ArticleNucleic acids research2000
Cloning of an interferon regulatory factor 2 isoform with different regulatory ability.
Article in Nucleic acids research, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 20 citations in OpenAlex.
- High-resolution functional annotation of human transcriptome: predicting isoform functions by a novel multiple instance-based label propagation method.Nucleic acids research · 2014Article
- The specificity of innate immune responses is enforced by repression of interferon response elements by NF-κB p50.Science signaling · 2011Article
- Molecular determinants and evolutionary dynamics of wobble splicing.Molecular biology and evolution · 2009Article
- Assessing the fraction of short-distance tandem splice sites under purifying selection.RNA (New York, N.Y.) · 2008Article
- Selection against tandem splice sites affecting structured protein regions.BMC evolutionary biology · 2008Article
- Manipulation of the toll-like receptor 7 signaling pathway by Epstein-Barr virus.Journal of virology · 2007Article
- Regulation of major histocompatibility complex class II gene expression in trophoblast cells.Reproductive biology and endocrinology : RB&E · 2004Review
- Identification of novel co-repressor molecules for Interferon Regulatory Factor-2.Nucleic acids research · 2003Article
- Impaired class II transactivator expression in mice lacking interferon regulatory factor-2.Oncogene · 2001Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Interferons (IFNs) are a family of multifunctional proteins involved in immune activation, regulation of cell growth and antiviral response. They exert their functions by induction of several IFN-stimulated genes, including IFN regulatory factors (IRFs), a family of transcriptional regulators. One of these factors, IRF-2, was initially cloned as an antagonistic counterpart to IRF-1 with oncogenic potential. Here we describe a second isoform of IRF-2, termed IRF-2s, cloned from human and murine cells. This isoform lacks two amino acids located C-terminal of the DNA-binding domain, which is conserved in all IRF family members, leading to a change in the predicted secondary structure. Both isoforms have similar binding affinities to known target sequences in electrophoretic mobility shift assays. Using reporter gene constructs with the type IV promoter region of the MHC class II transactivator (CIITA), which is the essential factor for IFN-gamma-induced MHC class II expression, we show that the short isoform IRF-2s exhibits a weaker activation ability compared to IRF-2. Thus, our data present the first evidence of two IRF-2 isoforms with different regulatory ability.
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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.