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FK506 binding protein 4, 59kDa

FKBP52, hsp56, FKBP59
The protein encoded by this gene is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. This encoded protein is a cis-trans prolyl isomerase that binds to the immunosuppressants FK506 and rapamycin. It has high structural and functional similarity to FK506-binding protein 1A (FKBP1A), but unlike FKBP1A, this protein does not have immunosuppressant activity when complexed with FK506. It interacts with interferon regulatory factor-4 and plays an important role in immunoregulatory gene expression in B and T lymphocytes. This encoded protein is known to associate with phytanoyl-CoA alpha-hydroxylase. It can also associate with two heat shock proteins (hsp90 and hsp70) and thus may play a role in the intracellular trafficking of hetero-oligomeric forms of the steroid hormone receptors. This protein correlates strongly with adeno-associated virus type 2 vectors (AAV) resulting in a significant increase in AAV-mediated transgene expression in human cell lines. Thus this encoded protein is thought to have important implications for the optimal use of AAV vectors in human gene therapy. The human genome contains several non-transcribed pseudogenes similar to this gene. [provided by RefSeq, Sep 2008] (from NCBI)
Top mentioned proteins: Hsp90, FKBP51, HSP70, CAN, CD1
Papers on FKBP52
Moving Beyond the Androgen Receptor (AR): Targeting AR-Interacting Proteins to Treat Prostate Cancer.
Mitsiades et al., Houston, United States. In Horm Cancer, Feb 2016
In this review, we discuss the preclinical research that has been done, as well as clinical trials for prostate cancer, on inhibiting several important families of AR-interacting proteins, including chaperones (such as heat shock protein 90 (HSP90) and FKBP52), pioneer factors (including forkhead box protein A1 (FOXA1) and GATA-2), and AR transcriptional coregulators such as the p160 steroid receptor coactivators (SRCs) SRC-1, SRC-2, SRC-3, as well as lysine deacetylases (KDACs) and lysine acetyltransferases (KATs).
Specific Binding of Tetratricopeptide Repeat Proteins to Heat Shock Protein 70 (Hsp70) and Heat Shock Protein 90 (Hsp90) Is Regulated by Affinity and Phosphorylation.
Gestwicki et al., Ann Arbor, United States. In Biochemistry, Jan 2016
To better understand these important protein-protein interactions on a wider scale, we measured the affinity of five TPR cochaperones, CHIP, Hop, DnaJC7, FKBP51, and FKBP52, for the C-termini of four members of the chaperone family, Hsc70, Hsp72, Hsp90α, and Hsp90β, in vitro.
Association study of androgen signaling pathway genes in polycystic ovary syndrome.
Goodarzi et al., Augusta, United States. In Fertil Steril, Nov 2015
CONCLUSION(S): Single-nucleotide polymorphisms in FKBP4, which codes for the AR co-chaperone FKBP52, may be associated with PCOS and body mass index in patients with PCOS.
Structure-Affinity Relationship Analysis of Selective FKBP51 Ligands.
Hausch et al., München, Germany. In J Med Chem, Nov 2015
The FK506-binding protein 51 (FKBP51) is a promising drug target for the treatment of stress-related psychiatric or metabolic disorders.
FKBP25 and FKBP38 regulate non-capacitative calcium entry through TRPC6.
Redondo et al., Cáceres, Spain. In Biochim Biophys Acta, Oct 2015
We have found interaction between FKBP38 and other FKBPs, like FKBP25, FKBP12, and FKBP52 that were not affected by FK506, as well as with calmodulin (CaM).
From steroid hormones to depressive states and senile dementias: New mechanistic, therapeutical and predictive approaches.
Baulieu, Le Kremlin-Bicêtre, France. In C R Biol, Aug 2015
Protein FKBP52 is involved in the dysfunction of the tau protein in Alzheimer's disease and senile dementias.
The joining of the Hsp90 and Hsp70 chaperone cycles yields transient interactions and stable intermediates: insights from mass spectrometry.
Robinson et al., Oxford, United Kingdom. In Oncotarget, Aug 2015
The Hsp70/Hsp90 chaperone cycles depend on the coordinated interplay of several co-chaperones including Hsp40, Hop and peptidyl-prolyl isomerases such as FKBP52.
Steroid Receptor-Associated Immunophilins: A Gateway to Steroid Signalling.
Ward et al., Australia. In Clin Biochem Rev, May 2015
The steroid receptor-associated immunophilins FKBP51, FKBP52, CyP40 and PP5 have specific roles in steroid receptor function that impact steroid hormone-binding affinity, nucleocytoplasmic shuttling and transcriptional activation of target genes in a tissue-specific manner.
Conformational Dynamics in FKBP Domains: Relevance to Molecular Signaling and Drug Design.
Hernandez et al., Albany, United States. In Curr Mol Pharmacol, 2014
Among the 22 FKBP domains in the human genome, FKBP12.6 and the first FKBP domains (FK1) of FKBP51 and FKBP52 are evolutionarily and structurally most similar to the archetypical FKBP12.
Steroid Receptor-Associated Immunophilins: Candidates for Diverse Drug-Targeting Approaches in Disease.
Ratajczak, Australia. In Curr Mol Pharmacol, 2014
The steroid receptor-associated TPR cochaperones FKBP51, FKBP52, CyP40 and PP5 have non-redundant roles in steroid receptor function that impact steroid hormone-binding affinity, nucleocyoplasmic shuttling and transcriptional activation of target genes in a tissue-specific manner.
Regulation of NF-κB signalling cascade by immunophilins.
Erlejman et al., Buenos Aires, Argentina. In Curr Mol Pharmacol, 2014
It was first discovered that TPR-domain immunophilins such as FKBP51 and FKBP52 play a cardinal role, usually in an antagonistic fashion, in the regulation of several members of the steroid receptor family via its interaction with the heat-shock protein of 90-kDa, Hsp90.
Chaperoning epigenetics: FKBP51 decreases the activity of DNMT1 and mediates epigenetic effects of the antidepressant paroxetine.
Rein et al., München, Germany. In Sci Signal, 2014
Epigenetic processes, such as DNA methylation, and molecular chaperones, including FK506-binding protein 51 (FKBP51), are independently implicated in stress-related mental disorders and antidepressant drug action.
FKBP4 is regulated by HOXA10 during decidualization and in endometriosis.
Taylor et al., New Haven, United States. In Reproduction, 2012
involved in the induction of decidualization
Proteomic approach reveals FKBP4 and S100A9 as potential prediction markers of therapeutic response to neoadjuvant chemotherapy in patients with breast cancer.
Lee et al., Seoul, South Korea. In J Proteome Res, 2012
Aimed to discover markers of drug resistance in breast cancer before neoadjuvant chemotherapy. Found FKBP4 and S100A9 might be putative prediction markers in discriminating the drug resistant group from the drug sensitive group of breast cancer patients.
Decrease of the immunophilin FKBP52 accumulation in human brains of Alzheimer's disease and FTDP-17.
Baulieu et al., Le Kremlin-Bicêtre, France. In J Alzheimers Dis, 2011
FKBP52 expression level is abnormally low in frontal cortex of Alzheimer's disease compared to controls.
Targeting the regulation of androgen receptor signaling by the heat shock protein 90 cochaperone FKBP52 in prostate cancer cells.
Cox et al., El Paso, United States. In Proc Natl Acad Sci U S A, 2011
FKBP52 regulates androgen receptor function through the BF3 surface.
Transgenic overexpression of HSP56 does not result in cardiac hypertrophy nor protect from ischaemia/reperfusion injury.
Townsend et al., London, United Kingdom. In Int J Biochem Cell Biol, 2011
Transgenic overexpression of HSP56 does not result in cardiac hypertrophy nor protect from ischaemia/reperfusion injury.
Posttranslational regulation of IRF-4 activity by the immunophilin FKBP52.
Hiscott et al., Montréal, Canada. In Immunity, 2000
In this study, we characterize a novel interaction between IRF-4 and the FK506-binding protein 52 (FKBP52), a 59 kDa member of the immunophilin family with peptidyl-prolyl isomerase activity (PPIase).
Steroid receptor interactions with heat shock protein and immunophilin chaperones.
Toft et al., Ann Arbor, United States. In Endocr Rev, 1997
Because the 9S receptor hsp90 heterocomplexes could be physically stabilized by molybdate, their protein composition could be readily studied, and it became clear that these complexes are multiprotein structures containing a number of unique proteins, such as FKBP51, FKBP52, CyP-40, and p23, that were discovered because of their presence in these structures.
Chaperone function of Hsp90-associated proteins.
Buchner et al., Regensburg, Germany. In Science, 1997
Two of the components, FKBP52 and p23, functioned as mechanistically distinct molecular chaperones.
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