ArticlePloS one2012
N-terminal domain of nuclear IL-1α shows structural similarity to the C-terminal domain of Snf1 and binds to the HAT/core module of the SAGA complex.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 28 citations in OpenAlex.
- Inflammatory responses following CRISPR modification of the nuclear localisation sequence in endogenous interleukin-1 alpha.Disease models & mechanisms · 2026Article
- Heparan sulfate fine-tuned interleukin-1 (IL-1) signaling inhibits insulin secretion of grafted pancreatic islets.Science advances · 2025Article
- Proximity labelling of pro-interleukin-1α reveals evolutionary conserved nuclear interactions.Nature communications · 2024Article
- Tumor Cell-Associated IL-1α Affects Breast Cancer Progression and Metastasis in Mice through Manipulation of the Tumor Immune Microenvironment.International journal of molecular sciences · 2024Article
- Analysis of the effects of importin α1 on the nuclear translocation of IL-1α in HeLa cells.Scientific reports · 2024Article
- The alarmin interleukin-1α causes preterm birth through the NLRP3 inflammasome.Molecular human reproduction · 2020Article
- Interleukin-1α associates with the tumor suppressor p53 following DNA damage.Scientific reports · 2020Article
- Identifying the Translatome of Mouse NEBD-Stage Oocytes via SSP-Profiling; A Novel Polysome Fractionation Method.International journal of molecular sciences · 2020Article
- Nuclear Alarmin Cytokines in Inflammation.Journal of immunology research · 2020Review
- Interleukin-1 as Innate Mediator of T Cell Immunity.Frontiers in immunology · 2020Review
- Uncoupling the Senescence-Associated Secretory Phenotype from Cell Cycle Exit via Interleukin-1 Inactivation Unveils Its Protumorigenic Role.Molecular and cellular biology · 2019Article
- Impact of Nuclear Interleukin-1 Alpha and EGFR Expression on Recurrence and Survival Outcomes in Oral Squamous Cell Carcinomas.Journal of oncology · 2019Article
- Redefining the ancestral origins of the interleukin-1 superfamily.Nature communications · 2018Article
- Function and regulation of IL-1α in inflammatory diseases and cancer.Immunological reviews · 2018Review
- Propiece IL-1α facilitates the growth of acute T-lymphocytic leukemia cells through the activation of NF-κB and SP1.Oncotarget · 2017Article
- HMGB1, IL-1α, IL-33 and S100 proteins: dual-function alarmins.Cellular & molecular immunology · 2017Review
- Distinct recruitment of human eIF4E isoforms to processing bodies and stress granules.BMC molecular biology · 2016Article
- Interleukin 1α and the inflammatory process.Nature immunology · 2016Review
- Association of interleukin 1 family with systemic sclerosis.Inflammation · 2014Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Interleukin-1α (IL-1α) is a proinflammatory cytokine and a key player in host immune responses in higher eukaryotes. IL-1α has pleiotropic effects on a wide range of cell types, and it has been extensively studied for its ability to contribute to various autoimmune and inflammation-linked disorders, including rheumatoid arthritis, Alzheimer's disease, systemic sclerosis and cardiovascular disorders. Interestingly, a significant proportion of IL-1α is translocated to the cell nucleus, in which it interacts with histone acetyltransferase complexes. Despite the importance of IL-1α, little is known regarding its binding targets and functions in the nucleus. We took advantage of the histone acetyltransferase (HAT) complexes being evolutionarily conserved from yeast to humans and the yeast SAGA complex serving as an epitome of the eukaryotic HAT complexes. Using gene knock-out technique and co-immunoprecipitation of the IL-1α precursor with TAP-tagged subunits of the yeast HAT complexes, we mapped the IL-1α-binding site to the HAT/Core module of the SAGA complex. We also predicted the 3-D structure of the IL-1α N-terminal domain, and by employing structure similarity searches, we found a similar structure in the C-terminal regulatory region of the catalytic subunit of the AMP-activated/Snf1 protein kinases, which interact with HAT complexes both in mammals and yeast, respectively. This finding is further supported with the ability of the IL-1α precursor to partially rescue growth defects of snf1Δ yeast strains on media containing 3-Amino-1,2,4-triazole (3-AT), a competitive inhibitor of His3. Finally, the careful evaluation of our data together with other published data in the field allows us to hypothesize a new function for the ADA complex in SAGA complex assembly.
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