ArticleProceedings of the National Academy of Sciences of the United States of America2006
The mutant leucine-zipper domain impairs both dimerization and suppressive function of Foxp3 in T cells.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 88 citations in OpenAlex.
- Review
- A splice of life: the discovery, function, and clinical implications of FOXP3 isoforms in autoimmune disease.International immunology · 2024Review
- Article
- Domain tethering impacts dimerization and DNA-mediated allostery in the human transcription factor FoxP1.The Journal of chemical physics · 2023Article
- FOXP3 Isoforms Expression in Cervical Cancer: Evidence about the Cancer-Related Properties of FOXP3Δ2Δ7 in Keratinocytes.Cancers · 2023Article
- Inhibition of FOXP3 by stapled alpha-helical peptides dampens regulatory T cell function.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- FOXP3 exon 2 controls TScience immunology · 2022Article
- The Importance of the Transcription Factor Foxp3 in the Development of Primary Immunodeficiencies.Journal of clinical medicine · 2022Review
- Obesity-related IL-18 Impairs T-Regulatory Cell Function and Promotes Lung Ischemia-Reperfusion Injury.American journal of respiratory and critical care medicine · 2021Article
- Searching for Peptide Inhibitors of T Regulatory Cell Activity by Targeting Specific Domains of FOXP3 Transcription Factor.Biomedicines · 2021Article
- Post-Translational Regulations of Foxp3 in Treg Cells and Their Therapeutic Applications.Frontiers in immunology · 2021Review
- A Structure-Guided Delineation of FOXP3 Regulation Mechanism in IPEX.Advances in experimental medicine and biology · 2021Article
- Disruption of FOXP3-EZH2 Interaction Represents a Pathobiological Mechanism in Intestinal Inflammation.Cellular and molecular gastroenterology and hepatology · 2019Article
- Characterization of a recurrent missense mutation in the forkhead DNA-binding domain of FOXP1.Scientific reports · 2018Article
- Alternative Splicing of FOXP3-Virtue and Vice.Frontiers in immunology · 2018Review
- Regulatory T Cells and Profile of FOXP3 Isoforms Expression in Peripheral Blood of Patients with Myelodysplastic Syndromes.Advances in hematology · 2018Article
- Therapeutic Potential of Gene-Modified Regulatory T Cells: From Bench to Bedside.Frontiers in immunology · 2018Review
- Article
- Protein-Protein Interaction Among the FoxP Family Members and their Regulation of Two Target Genes,Frontiers in molecular neuroscience · 2017Article
- Phase I study of azacitidine following donor lymphocyte infusion for relapsed acute myeloid leukemia post allogeneic stem cell transplantation.Leukemia research · 2016Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Regulatory T cells that express the Foxp3 transcription factor play important roles in preventing autoimmune diseases. Although several studies have demonstrated that the lack of the forkhead DNA-binding domain of Foxp3 caused severe autoimmune disease in scurfy mutant mice, the other functional domains of Foxp3 are less well characterized. Here, we show that the deletion of glutamic acid (DeltaE250) in the leucine-zipper domain of Foxp3 causes a loss of hyporesponsiveness when compared with wild-type Foxp3 upon antigenic stimulation. CD4 T cells that ectopically express the glutamic acid mutant show significant losses of suppressor activity both in vitro and in vivo. We also demonstrate that regulation of both Th1- and Th2-type cytokine secretion in CD4 T cells that express wild-type Foxp3 is significantly altered by the deletion of glutamic acid. Defects are also observed in the expression of adhesion molecules, such as l-selectin (CD62L) and CD103, suggesting an important role of glutamic acid in the migratory behavior of regulatory T cells. Finally, this mutation reduces transcriptional repressor activity and impairs the homodimerization of Foxp3. Taken together, our results provide insight into the mechanism that controls autoimmune diseases via the deletion of this single glutamic acid residue in the leucine-zipper domain of Foxp3.
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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.