ArticleNucleic acids research2015
FKBP51 employs both scaffold and isomerase functions to promote NF-κB activation in melanoma.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
44 citing papers in PubMed, 81 citations in OpenAlex.
- Combining Magnetic Resonance Imaging with Systemic Monocyte Evaluation for the Implementation of GBM Management.International journal of molecular sciences · 2021Trial
- Dual proximity-based interactome mapping of FKBP51 and FKBP52 uncovers shared metabolic networks.Biochemical and biophysical research communications · 2026Article
- FKBP5 isoforms shape immune pathways related to tumor tolerance.Cell death discovery · 2026Article
- Cannabidiol in Neurology: Current Insights and Translational Perspectives.Pharmaceuticals (Basel, Switzerland) · 2026Review
- miR‑100‑5p and miR‑203a‑3p suppress esophageal squamous cell carcinoma progression by targeting FKBP5.Oncology reports · 2025Article
- Review
- Exploring the potential of selective FKBP51 inhibitors on melanoma: an investigation of their in vitro and in vivo effects.Cell death discovery · 2025Article
- Role of FK506 binding protein 51 in central nervous system diseases.Frontiers in molecular neuroscience · 2025Review
- Expression and prognostic value of FKBP51 in Hodgkin lymphoma.Frontiers in immunology · 2025Article
- FKBP51 plays an essential role in Akt ubiquitination that requires Hsp90 and PHLPP.Cell death & disease · 2023Article
- Scaffold proteins of cancer signaling networks: The paradigm of FK506 binding protein 51 (FKBP51) supporting tumor intrinsic properties and immune escape.Oncology research · 2023Review
- Prenatal alcohol exposure alters mRNA expression for stress peptides, glucocorticoid receptor function and immune factors in acutely stressed neonatal brain.Frontiers in neuroscience · 2023Article
- Dexamethasone Sensitizes Acute Monocytic Leukemia Cells to Ara-C by Upregulating FKBP51.Frontiers in oncology · 2022Article
- IFI44 is an immune evasion biomarker for SARS-CoV-2 andFrontiers in immunology · 2022Article
- FKBP51 promotes invasion and migration by increasing the autophagic degradation of TIMP3 in clear cell renal cell carcinoma.Cell death & disease · 2021Article
- Article
- FKBP51 Affects TNF-Related Apoptosis Inducing Ligand Response in Melanoma.Frontiers in cell and developmental biology · 2021Article
- Discovery of pentapeptide-inhibitor hits targeting FKBP51 by combining computational modeling and X-ray crystallography.Computational and structural biotechnology journal · 2021Article
- Sex and Gender Disparities in Melanoma.Cancers · 2020Review
- Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 3 countries.
Funding
Abstract
Melanoma is the most aggressive skin cancer; its prognosis, particularly in advanced stages, is disappointing largely due to the resistance to conventional anticancer treatments and high metastatic potential. NF-κB constitutive activation is a major factor for the apoptosis resistance of melanoma. Several studies suggest a role for the immunophilin FKBP51 in NF-κB activation, but the underlying mechanism is still unknown. In the present study, we demonstrate that FKBP51 physically interacts with IKK subunits, and facilitates IKK complex assembly. FKBP51-knockdown inhibits the binding of IKKγ to the IKK catalytic subunits, IKK-α and -β, and attenuates the IKK catalytic activity. Using FK506, an inhibitor of the FKBP51 isomerase activity, we found that the IKK-regulatory role of FKBP51 involves both its scaffold function and its isomerase activity. Moreover, FKBP51 also interacts with TRAF2, an upstream mediator of IKK activation. Interestingly, both FKBP51 TPR and PPIase domains are required for its interaction with TRAF2 and IKKγ, whereas only the TPR domain is involved in interactions with IKKα and β. Collectively, these results suggest that FKBP51 promotes NF-κB activation by serving as an IKK scaffold as well as an isomerase. Our findings have profound implications for designing novel melanoma therapies based on modulation of FKBP51.
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What OpenQuestion holds
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.