ArticleThe Journal of biological chemistry2011
The type III histone deacetylase Sirt1 protein suppresses p300-mediated histone H3 lysine 56 acetylation at Bclaf1 promoter to inhibit T cell activation.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
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Who cites it
67 citing papers in PubMed, 96 citations in OpenAlex.
- Single-cell multi-omics dissects transcript isoform and immune repertoire dynamics in human immunosenescence.Science China. Life sciences · 2026Article
- Isoquercitrin suppresses neuronal ferroptosis in ischemic stroke via SIRT1-mediated deacetylation of H3K9 at the RBM15 promoter.Daru : journal of Faculty of Pharmacy, Tehran University of Medical Sciences · 2026Article
- Article
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- The Role of Hepatic SIRT1: From Metabolic Regulation to Immune Modulation and Multi-target Therapeutic Strategies.Journal of clinical and translational hepatology · 2025Review
- Regulatory Dynamics of Nrf2 With Sirtuins in the Brain: Exploring Cellular Metabolism, Synaptic Plasticity, and Defense Mechanisms.Journal of neurochemistry · 2025Review
- p85β acts as a transcription cofactor and cooperates with BCLAF1 in the nucleus.Nature communications · 2025Article
- Ionizing radiation-induced disruption of Rela-Bclaf1-spliceosome regulatory axis in primary spermatocytes causing spermatogenesis dysfunction.Cell communication and signaling : CCS · 2025Article
- Targeting NAD+ Metabolism to Modulate Autoimmunity and Inflammation.Journal of immunology (Baltimore, Md. : 1950) · 2024Review
- Inhibition of CD38 enzymatic activity enhances CAR-T cell immune-therapeutic efficacy by repressing glycolytic metabolism.Cell reports. Medicine · 2024Article
- Article
- Recurrent somatic mutations as predictors of immunotherapy response.Nature communications · 2022Article
- Fatty acids derived from apoptotic chondrocytes fuel macrophages FAO through MSR1 for facilitating BMSCs osteogenic differentiation.Redox biology · 2022Article
- Sirtuins are crucial regulators of T cell metabolism and functions.Experimental & molecular medicine · 2022Review
- Function of BCLAF1 in human disease.Oncology letters · 2022Review
- The Redox-Metabolic Couple of T Lymphocytes: Potential Consequences for Hypertension.Antioxidants & redox signaling · 2021Review
- The long noncoding RNA lncCIRBIL disrupts the nuclear translocation of Bclaf1 alleviating cardiac ischemia-reperfusion injury.Nature communications · 2021Article
- The Role of Sirtuin-1 in Immune Response and Systemic Lupus Erythematosus.Frontiers in immunology · 2021Review
- SIRT1: A Potential Therapeutic Target in Autoimmune Diseases.Frontiers in immunology · 2021Review
- Metabolic signaling in T cells.Cell research · 2020Review
7 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The NAD-dependent histone deacetylase Sirt1 is a negative regulator of T cell activation. Here we report that Sirt1 inhibits T cell activation by suppressing the transcription of Bcl2-associated factor 1 (Bclaf1), a protein required for T cell activation. Sirt1-null T cells have increased acetylation of the histone 3 lysine 56 residue (H3K56) at the bclaf1 promoter, as well as increasing Bclaf1 transcription. Sirt1 binds to bclaf1 promoter upon T cell receptor (TCR)/CD28 stimulation by forming a complex with histone acetyltransferase p300 and NF-κB transcription factor Rel-A. The recruitment of Sirt1, but not p300, requires Rel-A because blocking Rel-A nuclear translocation in T cells and siRNA-mediated knockdown of Rel-A can inhibit Sirt1 binding to bclaf1 promoter. Although knockdown of either p300 or GCN5 partially suppressed global H3K56 acetylation, only p300 knockdown specifically attenuated H3K56 acetylation at the bclaf1 promoter. Lastly, knockdown of Bclaf1 suppresses the hyperactivation observed in Sirt1(-/-) T cells, indicated by less IL-2 production in CD4(+) T cells and reduced proliferation. Therefore, Sirt1 negatively regulates T cell activation via H3K56 deacetylation at the promoter region to inhibit transcription of Bclaf1.
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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.