ArticleThe Journal of biological chemistry2014
NF-κB transcriptional activity is modulated by FK506-binding proteins FKBP51 and FKBP52: a role for peptidyl-prolyl isomerase activity.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed, 98 citations in OpenAlex.
- Dual proximity-based interactome mapping of FKBP51 and FKBP52 uncovers shared metabolic networks.Biochemical and biophysical research communications · 2026Article
- Mechanistic insights into PFAS-induced effects on B lymphocyte activation and antibody secretion.Archives of toxicology · 2026Article
- Identification of reactive CpGs and RNA expression in early COVID-19 through cis-eQTM analysis reflecting disease severity and recovery.Communications biology · 2025Article
- Childhood exposure to danger increases Black youths' alcohol consumption, accelerated aging, and cardiac risk as young adults: A test of the incubation hypothesis.Development and psychopathology · 2025Article
- Role of FK506 binding protein 51 in central nervous system diseases.Frontiers in molecular neuroscience · 2025Review
- Early-life obesogenic environment integrates immunometabolic and epigenetic signatures governing neuroinflammation.Brain, behavior, & immunity - health · 2024Article
- Article
- NFAT activation by FKBP52 promotes cancer cell proliferation by suppressing p53.Life science alliance · 2024Article
- LncRNA-mediated ceRNA network reveals the mechanism of action of Saorilao-4 decoction against pulmonary fibrosis.Frontiers in genetics · 2024Article
- Skin Anti-Inflammatory Potential with Reduced Side Effects of Novel Glucocorticoid Receptor Agonists.International journal of molecular sciences · 2023Article
- Changes in the Proteome of Platelets from Patients with Critical Progression of COVID-19.Cells · 2023Article
- Impact of FKBP52 on cell proliferation and hormone-dependent cancers.Cancer science · 2023Review
- Scaffold proteins of cancer signaling networks: The paradigm of FK506 binding protein 51 (FKBP51) supporting tumor intrinsic properties and immune escape.Oncology research · 2023Review
- Role of FKBP5 and its genetic mutations in stress-induced psychiatric disorders: an opportunity for drug discovery.Frontiers in psychiatry · 2023Review
- Inhibition of FKBP51 induces stress resilience and alters hippocampal neurogenesis.Molecular psychiatry · 2022Article
- The Scaffold Immunophilin FKBP51 Is a Phosphoprotein That Undergoes Dynamic Mitochondrial-Nuclear Shuttling.Cells · 2022Article
- Methylation of FKBP5 is associated with accelerated DNA methylation ageing and cardiometabolic risk: replication in young-adult and middle-aged Black Americans.Epigenetics · 2022Article
- The maternal-placental-fetal interface: Adaptations of the HPA axis and immune mediators following maternal stress and prenatal alcohol exposure.Experimental neurology · 2022Review
- Article
- Childhood adversity predicts black young adults' DNA methylation-based accelerated aging: A dual pathway model.Development and psychopathology · 2022Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Hsp90 binding immunophilins FKBP51 and FKBP52 modulate steroid receptor trafficking and hormone-dependent biological responses. With the purpose to expand this model to other nuclear factors that are also subject to nuclear-cytoplasmic shuttling, we analyzed whether these immunophilins modulate NF-κB signaling. It is demonstrated that FKBP51 impairs both the nuclear translocation rate of NF-κB and its transcriptional activity. The inhibitory action of FKBP51 requires neither the peptidylprolyl-isomerase activity of the immunophilin nor its association with Hsp90. The TPR domain of FKBP51 is essential. On the other hand, FKBP52 favors the nuclear retention time of RelA, its association to a DNA consensus binding sequence, and NF-κB transcriptional activity, the latter effect being strongly dependent on the peptidylprolyl-isomerase activity and also on the TPR domain of FKBP52, but its interaction with Hsp90 is not required. In unstimulated cells, FKBP51 forms endogenous complexes with cytoplasmic RelA. Upon cell stimulation with phorbol ester, the NF-κB soluble complex exchanges FKBP51 for FKBP52, and the NF-κB biological effect is triggered. Importantly, FKBP52 is functionally recruited to the promoter region of NF-κB target genes, whereas FKBP51 is released. Competition assays demonstrated that both immunophilins antagonize one another, and binding assays with purified proteins suggest that the association of RelA and immunophilins could be direct. These observations suggest that the biological action of NF-κB in different cell types could be positively regulated by a high FKBP52/FKBP51 expression ratio by favoring NF-κB nuclear retention, recruitment to the promoter regions of target genes, and transcriptional activity.
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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.