Interaction between Interferon Consensus Sequence-binding Protein and COP9/Signalosome Subunit CSN2 (Trip15)
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Interferon consensus sequence-binding protein (ICSBP) is a member of the interferon regulatory factors (IRF) that has a pivotal role in mediating resistance to pathogenic infections in mice and in promoting the differentiation of myeloid cells. ICSBP exerts some of its transcriptional activities via association with other factors that enable its binding to a variety of promoters containing DNA composite elements. These interactions are mediated through a specific COOH-terminal domain termed IAD (IRF association domain). To gain a broader insight of the capacity of ICSBP to interact with other factors, yeast two-hybrid screens were performed using ICSBP-IAD as a bait against a B-cell cDNA library. Trip15 was identified as a specific interacting factor with ICSBP in yeast cells, which was also confirmed by in vitro glutathione S-transferase pull-down assays and by coimmunoprecipitation studies in COS7 cells. Trip15 was recently identified as a component of the COP9/signalosome (CSN) complex composed of eight evolutionary conserved subunits and thus termed CSN2. This complex has a role in cell-signaling processes, which is manifested by its associated novel kinase activity and by the involvement of its subunits in regulating multiple cell-signaling pathways and cell-cycle progression. We show that in vitro association of ICSBP with the CSN leads to phosphorylation of ICSBP at a unique serine residue within its IAD. The phosphorylated residue is essential for efficient association with IRF-1 and thus for the repressor activity of ICSBP exerted on IRF-1. This suggests that the CSN has a role in integrating incoming signals that affect the transcriptional activity of ICSBP.
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ICSBP binds Trip15 (CSN2), a component of the COP9/signalosome (CSN) complex, and the CSN complex phosphorylates a serine residue within the IAD of ICSBP that is essential for efficient association with IRF-1.
“ICSBP was shown to bind Trip15 (CSN2), which is a component of the COP9/signalosome (CSN) complex.”
From Review: ICSBP/IRF-8: Its Regulatory Roles in the Development of Myeloid Cells (2002) · cites this paper as [36]
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- Authors
- Cohen, H., Azriel, A., Cohen, T., Meraro, D., Hashmueli, S., Bech-Otschir, D., Kraft, R., Dubiel, W., & Levi, B.-Z.
- Affiliations
- Technion – Israel Institute of Technology (IL)
- Max Delbrück Center (DE)
- Humboldt-Universität zu Berlin (DE)
- Corresponding author
- Levi, Ben-Zion
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-12
- Volume
- 275
- Issue
- 50
- Pages
- 39081-39089
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2135480993
- Cited by
- 45
- References
- 51
- Citations by year
- 2022: 1 · 2021: 1 · 2019: 1 · 2018: 1 · 2016: 2 · 2015: 1 · 2014: 1 · 2013: 1 · 2012: 1
- FWCI
- 2.71
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- IRF1, COP9 signalosome, β-casein, protein-protein interaction, serine phosphorylation, transcriptional repression, interferon regulatory factors, signal integration
- MeSH terms
- COP9 Signalosome Complex, Interferon Regulatory Factor-8, Alanine, Animals, B-Lymphocytes, Carrier Proteins, DNA, Dose-Response Relationship, Drug, Glutathione Transferase, HeLa Cells, Humans, Models, Biological, Nuclear Proteins, Peptide Hydrolases, Phosphorylation, Plasmids, Precipitin Tests, Promoter Regions, Genetic, Protein Binding, Proteins, Receptors, Thyroid Hormone, Repressor Proteins, RNA, Messenger, Serine, Transcription Factors, Transcription, Genetic, Blotting, Northern, Signal Transduction, Gene Library, Mutagenesis, Site-Directed, 3T3 Cells, Protein Structure, Tertiary, DNA, Complementary, HL-60 Cells, COS Cells, Two-Hybrid System Techniques, Multiprotein Complexes, Interferon Regulatory Factors, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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