FKBP1B

Summary

Gene Symbol: FKBP1B
Description: FK506 binding protein 1B
Alias: FKBP12.6, FKBP1L, OTK4, PKBP1L, PPIase, peptidyl-prolyl cis-trans isomerase FKBP1B, 12.6 kDa FK506-binding protein, 12.6 kDa FKBP, FK506 binding protein 1B, 12.6 kDa, FK506-binding protein 12.6, FKBP-12.6, FKBP-1B, PPIase FKBP1B, calstabin 2, h-FKBP-12, immunophilin FKBP12.6, rotamase
Species: human
Products:     FKBP1B

Top Publications

  1. Jeyakumar L, Ballester L, Cheng D, McIntyre J, Chang P, Olivey H, et al. FKBP binding characteristics of cardiac microsomes from diverse vertebrates. Biochem Biophys Res Commun. 2001;281:979-86 pubmed publisher
    ..6. Dog is the exception. It can now be concluded that the association of FKBP isoforms with RyR2 is widely conserved in the hearts of different species of vertebrates...
  2. Cornea R, Nitu F, Samso M, Thomas D, Fruen B. Mapping the ryanodine receptor FK506-binding protein subunit using fluorescence resonance energy transfer. J Biol Chem. 2010;285:19219-26 pubmed publisher
    ..FRET mapping of RyR-bound FKBP12.6 is consistent with the predictions of a previous cryoelectron microscopy study and strongly supports the proposed structural model. ..
  3. Tiso N, Salamon M, Bagattin A, Danieli G, Argenton F, Bortolussi M. The binding of the RyR2 calcium channel to its gating protein FKBP12.6 is oppositely affected by ARVD2 and VTSIP mutations. Biochem Biophys Res Commun. 2002;299:594-8 pubmed
    ..We also provide evidence of the suitability of this system to test new drugs that target RyRs-FKBP12s interactions and do not affect yeast growth. ..
  4. Geisler M, Kolukisaoglu H, Bouchard R, Billion K, Berger J, Saal B, et al. TWISTED DWARF1, a unique plasma membrane-anchored immunophilin-like protein, interacts with Arabidopsis multidrug resistance-like transporters AtPGP1 and AtPGP19. Mol Biol Cell. 2003;14:4238-49 pubmed
    ..Heterologously expressed TWD1 does not exhibit cis-trans-peptidylprolyl isomerase (PPIase) activity and does not complement yeast FKBP12 mutants, suggesting that TWD1 acts indirectly via protein-protein ..
  5. Zissimopoulos S, Lai F. Interaction of FKBP12.6 with the cardiac ryanodine receptor C-terminal domain. J Biol Chem. 2005;280:5475-85 pubmed
    ..6 may be present at the RyR2 C terminus, proximal to the channel pore, a sterically appropriate location that would enable this protein to play a central role in the modulation of this critical ion channel. ..
  6. Sui Y, Fu X, Wang Y, Hu W, Zhang T, Liu W, et al. Expression, purification and characterization of a catalytic domain of human protein tyrosine phosphatase non-receptor 12 (PTPN12) in Escherichia coli with FKBP-type PPIase as a chaperon. Protein Expr Purif. 2018;142:45-52 pubmed publisher
    ....
  7. Wang R, Zhong X, Meng X, Koop A, Tian X, Jones P, et al. Localization of the dantrolene-binding sequence near the FK506-binding protein-binding site in the three-dimensional structure of the ryanodine receptor. J Biol Chem. 2011;286:12202-12 pubmed publisher
    ..6-binding site but distant to the central region around residue Ser-2367. An allosteric mechanism by which dantrolene stabilizes interdomain interactions between the NH2-terminal and central regions is proposed. ..
  8. Guo T, Cornea R, Huke S, Camors E, Yang Y, Picht E, et al. Kinetics of FKBP12.6 binding to ryanodine receptors in permeabilized cardiac myocytes and effects on Ca sparks. Circ Res. 2010;106:1743-52 pubmed publisher
    ..6-RyR2 association and activate RyR2. However, the function of FKBP12.6/12 and role of PKA phosphorylation in cardiac myocytes are controversial...
  9. Zissimopoulos S, Thomas N, Jamaluddin W, Lai F. FKBP12.6 binding of ryanodine receptors carrying mutations associated with arrhythmogenic cardiac disease. Biochem J. 2009;419:273-8 pubmed publisher
    ..6 binding, but to the same extent as for the wild-type. Our findings suggest that FKBP12.6 regulation of RyR2 is unlikely to be the primary defect in inherited arrhythmogenic cardiac disease...
  10. Xiao J, Tian X, Jones P, Bolstad J, Kong H, Wang R, et al. Removal of FKBP12.6 does not alter the conductance and activation of the cardiac ryanodine receptor or the susceptibility to stress-induced ventricular arrhythmias. J Biol Chem. 2007;282:34828-38 pubmed
    ..Collectively, our results demonstrate that the loss of FKBP12.6 has no significant effect on the conduction and activation of RyR2 or the propensity for spontaneous Ca(2+) release and stress-induced ventricular arrhythmias. ..

Detail Information

Publications62

  1. Jeyakumar L, Ballester L, Cheng D, McIntyre J, Chang P, Olivey H, et al. FKBP binding characteristics of cardiac microsomes from diverse vertebrates. Biochem Biophys Res Commun. 2001;281:979-86 pubmed publisher
    ..6. Dog is the exception. It can now be concluded that the association of FKBP isoforms with RyR2 is widely conserved in the hearts of different species of vertebrates...
  2. Cornea R, Nitu F, Samso M, Thomas D, Fruen B. Mapping the ryanodine receptor FK506-binding protein subunit using fluorescence resonance energy transfer. J Biol Chem. 2010;285:19219-26 pubmed publisher
    ..FRET mapping of RyR-bound FKBP12.6 is consistent with the predictions of a previous cryoelectron microscopy study and strongly supports the proposed structural model. ..
  3. Tiso N, Salamon M, Bagattin A, Danieli G, Argenton F, Bortolussi M. The binding of the RyR2 calcium channel to its gating protein FKBP12.6 is oppositely affected by ARVD2 and VTSIP mutations. Biochem Biophys Res Commun. 2002;299:594-8 pubmed
    ..We also provide evidence of the suitability of this system to test new drugs that target RyRs-FKBP12s interactions and do not affect yeast growth. ..
  4. Geisler M, Kolukisaoglu H, Bouchard R, Billion K, Berger J, Saal B, et al. TWISTED DWARF1, a unique plasma membrane-anchored immunophilin-like protein, interacts with Arabidopsis multidrug resistance-like transporters AtPGP1 and AtPGP19. Mol Biol Cell. 2003;14:4238-49 pubmed
    ..Heterologously expressed TWD1 does not exhibit cis-trans-peptidylprolyl isomerase (PPIase) activity and does not complement yeast FKBP12 mutants, suggesting that TWD1 acts indirectly via protein-protein ..
  5. Zissimopoulos S, Lai F. Interaction of FKBP12.6 with the cardiac ryanodine receptor C-terminal domain. J Biol Chem. 2005;280:5475-85 pubmed
    ..6 may be present at the RyR2 C terminus, proximal to the channel pore, a sterically appropriate location that would enable this protein to play a central role in the modulation of this critical ion channel. ..
  6. Sui Y, Fu X, Wang Y, Hu W, Zhang T, Liu W, et al. Expression, purification and characterization of a catalytic domain of human protein tyrosine phosphatase non-receptor 12 (PTPN12) in Escherichia coli with FKBP-type PPIase as a chaperon. Protein Expr Purif. 2018;142:45-52 pubmed publisher
    ....
  7. Wang R, Zhong X, Meng X, Koop A, Tian X, Jones P, et al. Localization of the dantrolene-binding sequence near the FK506-binding protein-binding site in the three-dimensional structure of the ryanodine receptor. J Biol Chem. 2011;286:12202-12 pubmed publisher
    ..6-binding site but distant to the central region around residue Ser-2367. An allosteric mechanism by which dantrolene stabilizes interdomain interactions between the NH2-terminal and central regions is proposed. ..
  8. Guo T, Cornea R, Huke S, Camors E, Yang Y, Picht E, et al. Kinetics of FKBP12.6 binding to ryanodine receptors in permeabilized cardiac myocytes and effects on Ca sparks. Circ Res. 2010;106:1743-52 pubmed publisher
    ..6-RyR2 association and activate RyR2. However, the function of FKBP12.6/12 and role of PKA phosphorylation in cardiac myocytes are controversial...
  9. Zissimopoulos S, Thomas N, Jamaluddin W, Lai F. FKBP12.6 binding of ryanodine receptors carrying mutations associated with arrhythmogenic cardiac disease. Biochem J. 2009;419:273-8 pubmed publisher
    ..6 binding, but to the same extent as for the wild-type. Our findings suggest that FKBP12.6 regulation of RyR2 is unlikely to be the primary defect in inherited arrhythmogenic cardiac disease...
  10. Xiao J, Tian X, Jones P, Bolstad J, Kong H, Wang R, et al. Removal of FKBP12.6 does not alter the conductance and activation of the cardiac ryanodine receptor or the susceptibility to stress-induced ventricular arrhythmias. J Biol Chem. 2007;282:34828-38 pubmed
    ..Collectively, our results demonstrate that the loss of FKBP12.6 has no significant effect on the conduction and activation of RyR2 or the propensity for spontaneous Ca(2+) release and stress-induced ventricular arrhythmias. ..
  11. Pandya M, Liu H, Dangaria S, Zhu W, Li L, Pan S, et al. Integrative Temporo-Spatial, Mineralogic, Spectroscopic, and Proteomic Analysis of Postnatal Enamel Development in Teeth with Limited Growth. Front Physiol. 2017;8:793 pubmed publisher
    ..Together, this study provides a baseline for a comprehensive understanding of the mineralogic and proteomic events that contribute to the complexity of mammalian tooth enamel development...
  12. Shimizu T, Uchida C, Shimizu R, Motohashi H, Uchida T. Prolyl isomerase Pin1 promotes proplatelet formation of megakaryocytes via tau. Biochem Biophys Res Commun. 2017;493:946-951 pubmed publisher
    ..Pin1 bound tau and promoted microtubule polymerization. Our results show that Pin1 serves as a positive regulatory molecule of proplatelet formation of MKs by enhancing the function of phosphorylated tau. ..
  13. Kozlov G, Muñoz Escobar J, Castro K, Gehring K. Mapping the ER Interactome: The P Domains of Calnexin and Calreticulin as Plurivalent Adapters for Foldases and Chaperones. Structure. 2017;25:1415-1422.e3 pubmed publisher
    ..The structural diversity of the accessory factors suggests that these chaperones became specialized for glycoprotein folding through convergent evolution of their P-domain binding sites. ..
  14. Krapp S, Schuy C, Greiner E, Stephan I, Alberter B, Funk C, et al. Begomoviral Movement Protein Effects in Human and Plant Cells: Towards New Potential Interaction Partners. Viruses. 2017;9: pubmed publisher
    ..Possible roles of these putative interaction partners in the begomoviral life cycle and cytoskeletal association modes are discussed...
  15. Zhao H, Cui G, Jin J, Chen X, Xu B. Synthesis and Pin1 inhibitory activity of thiazole derivatives. Bioorg Med Chem. 2016;24:5911-5920 pubmed publisher
    Pin1 (Protein interacting with NIMA1) is a peptidyl prolyl cis-trans isomerase (PPIase) which specifically catalyze the conformational conversion of the amide bond of pSer/Thr-Pro motifs in its substrate proteins and is a novel promising ..
  16. Masumiya H, Wang R, Zhang J, Xiao B, Chen S. Localization of the 12.6-kDa FK506-binding protein (FKBP12.6) binding site to the NH2-terminal domain of the cardiac Ca2+ release channel (ryanodine receptor). J Biol Chem. 2003;278:3786-92 pubmed
    ..6 binding. These data suggest that FKBP12.6 binding is likely to be conformationdependent. Binding of FKBP12.6 to the NH(2)-terminal domain may play a role in stabilizing the conformation of this region. ..
  17. Zhu Y, Gong Y, Li A, Chen M, Kang D, Liu J, et al. Differential Proteomic Analysis Reveals Protein Networks and Pathways that May Contribute to Helicobacter pylori FKBP-Type PPIase-Associated Gastric Diseases. Proteomics Clin Appl. 2017;: pubmed publisher
    ..pylori gene, peptidylprolyl isomerase-FK506 binding protein (PPIase-FKBP), and showed that PPIase-FKBP was capable of inducing oncogenic transformation of gastric epithelial cells...
  18. Marx S, Reiken S, Hisamatsu Y, Jayaraman T, Burkhoff D, Rosemblit N, et al. PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts. Cell. 2000;101:365-76 pubmed
    ..6, PKA, the protein phosphatases PP1 and PP2A, and an anchoring protein, mAKAP. In failing human hearts, RyR2 is PKA hyperphosphorylated, resulting in defective channel function due to increased sensitivity to Ca2+-induced activation. ..
  19. Qiao X, Liu Y, Luo L, Chen L, Zhao C, Ai X. Effects of naturally occurring charged mutations on the structure, stability, and binding of the Pin1 WW domain. Biochem Biophys Res Commun. 2017;487:470-476 pubmed publisher
    ..Considering that the WW domain participates in the catalytic activity of the Pin1 isomerase, our study represents a novel approach for studying Pin1 function through the analysis of its naturally occurring mutants...
  20. Noguchi N, Takasawa S, Nata K, Tohgo A, Kato I, Ikehata F, et al. Cyclic ADP-ribose binds to FK506-binding protein 12.6 to release Ca2+ from islet microsomes. J Biol Chem. 1997;272:3133-6 pubmed
    ..6 did not show Ca2+ release by cADPR. These results strongly suggest that cADPR may be the ligand for FKBP12.6 in islet RyR and that the binding of cADPR to FKBP12.6 frees the RyR from FKBP12.6, causing it to release Ca2+. ..
  21. Bacchi M, Jullian M, Sirigu S, Fould B, Huet T, Bruyand L, et al. Total chemical synthesis, refolding, and crystallographic structure of fully active immunophilin calstabin 2 (FKBP12.6). Protein Sci. 2016;25:2225-2242 pubmed publisher
    ....
  22. Csizmok V, Montecchio M, Lin H, Tyers M, Sunnerhagen M, Forman Kay J. Multivalent Interactions with Fbw7 and Pin1 Facilitate Recognition of c-Jun by the SCFFbw7 Ubiquitin Ligase. Structure. 2017;: pubmed publisher
    ..We show that the Pin1 WW and PPIase domains interact in a dynamic complex with multiply phosphorylated c-Jun...
  23. O Brien F, Venturi E, Sitsapesan R. The ryanodine receptor provides high throughput Ca2+-release but is precisely regulated by networks of associated proteins: a focus on proteins relevant to phosphorylation. Biochem Soc Trans. 2015;43:426-33 pubmed publisher
    ....
  24. Vivoli M, Renou J, Chevalier A, Norville I, Diaz S, Juli C, et al. A miniaturized peptidyl-prolyl isomerase enzyme assay. Anal Biochem. 2017;536:59-68 pubmed publisher
    ..g. cardiovascular disease, cancer and Alzheimer's. The development of novel PPIase inhibitors has been limited by the lack of a rapid, laboratory-based assay for these enzymes, as their substrates ..
  25. Galat A. Peptidylprolyl Isomerases as In Vivo Carriers for Drugs That Target Various Intracellular Entities. Biomolecules. 2017;7: pubmed publisher
    ..These three attributes enhance binding of PPIase/pharmacophore complexes to diverse intracellular entities, some of which perturb signalization pathways causing ..
  26. Artier J, da Silva Zandonadi F, de Souza Carvalho F, Pauletti B, Leme A, Carnielli C, et al. Comparative proteomic analysis of Xanthomonas citri ssp. citri periplasmic proteins reveals changes in cellular envelope metabolism during in vitro pathogenicity induction. Mol Plant Pathol. 2018;19:143-157 pubmed publisher
    ..The results present new potential targets against XAC to be investigated in further functional studies...
  27. Haokip N, Naorem A. Functional characterisation of parvulin-type peptidyl prolyl cis-trans isomerase, PinA in Dictyostelium discoideum. Biochem Biophys Res Commun. 2017;482:208-214 pubmed publisher
    ..We conclude that PinA is required for normal growth as well as development in D. discoideum...
  28. Skagia A, Zografou C, Venieraki A, Fasseas C, Katinakis P, Dimou M. Functional analysis of the cyclophilin PpiB role in bacterial cell division. Genes Cells. 2017;22:810-824 pubmed publisher
    Escherichia coli PpiB is a peptidyl-prolyl cis/trans isomerase (PPIase, EC: 5.2.1.8) with chaperone activity...
  29. Liu Y, Chen H, Ji G, Li B, Mohler P, Zhu Z, et al. Transgenic analysis of the role of FKBP12.6 in cardiac function and intracellular calcium release. Assay Drug Dev Technol. 2011;9:620-7 pubmed publisher
    ..MHC-FKBP12.6 mice displayed normal cardiac development and function. We demonstrated that MHC-FKBP12.6 mice are able to rescue abnormal cardiac hypertrophy and abnormal calcium release in FKBP12.6-deficient mice...
  30. Zhang H, Wang J, Li S, Wang S, Liu M, Wang W, et al. Molecular cloning, expression, purification and functional characterization of an antifungal cyclophilin protein from Panax ginseng. Biomed Rep. 2017;7:527-531 pubmed publisher
    ..In addition, pgCyP showed high PPIase activity...
  31. George C, Sorathia R, Bertrand B, Lai F. In situ modulation of the human cardiac ryanodine receptor (hRyR2) by FKBP12.6. Biochem J. 2003;370:579-89 pubmed
    ..6 on hRyR2-mediated intracellular Ca(2+) handling could be antagonized using rapamycin (5 microM). These results suggest that FKBP12.6 associates with hRyR2 in situ to modulate precisely the functionality of hRyR2 Ca(2+)-release channel. ..
  32. Wehrens X, Lehnart S, Reiken S, van der Nagel R, Morales R, Sun J, et al. Enhancing calstabin binding to ryanodine receptors improves cardiac and skeletal muscle function in heart failure. Proc Natl Acad Sci U S A. 2005;102:9607-12 pubmed
    ..We conclude that JTV519 may provide a specific way to treat the cardiac and skeletal muscle myopathy in HF by increasing calstabin binding to RyR. ..
  33. Villmow M, Baumann M, Malesevic M, Sachs R, Hause G, Fändrich M, et al. Inhibition of Aβ(1-40) fibril formation by cyclophilins. Biochem J. 2016;473:1355-68 pubmed publisher
    ....
  34. Zhang J, Waddell H, Wu E, Dholakia J, Okolo C, McLay J, et al. FKBPs facilitate the termination of spontaneous Ca2+ release in wild-type RyR2 but not CPVT mutant RyR2. Biochem J. 2016;473:2049-60 pubmed publisher
    ..The inability of FKBPs to mediate a similar effect on the mutant RyR2 represents a novel mechanism by which mutations within RyR2 lead to arrhythmia...
  35. Ernst K, Schnell L, Barth H. Host Cell Chaperones Hsp70/Hsp90 and Peptidyl-Prolyl Cis/Trans Isomerases Are Required for the Membrane Translocation of Bacterial ADP-Ribosylating Toxins. Curr Top Microbiol Immunol. 2017;406:163-198 pubmed publisher
    ..cell chaperones including Hsp90 and protein-folding helper enzymes of the peptidyl-prolyl cis/trans isomerase (PPIase) type facilitate this membrane translocation of the unfolded A-domain for ADP-ribosylating toxins but not for ..
  36. Vervliet T, Parys J, Bultynck G. Bcl-2 and FKBP12 bind to IP3 and ryanodine receptors at overlapping sites: the complexity of protein-protein interactions for channel regulation. Biochem Soc Trans. 2015;43:396-404 pubmed publisher
    ....
  37. Wang L, Wang X, Ren Z, Tang W, Zou Q, Wang J, et al. Oxidative Folding of Conopeptides Modified by Conus Protein Disulfide Isomerase. Protein J. 2017;36:407-416 pubmed publisher
    ..Thus, conus protein disulfide isomerase functions not only as an enzyme that catalyses oxidative process but also a fusion partner in recombinant conotoxin expression. ..
  38. Zissimopoulos S, Docrat N, Lai F. Redox sensitivity of the ryanodine receptor interaction with FK506-binding protein. J Biol Chem. 2007;282:6976-83 pubmed
    ..6 dissociation from the RyR2 channel complex, did not restore normal FKBP binding under oxidizing conditions. Our results indicate that the redox state of the RyR is intimately connected with FKBP binding affinity. ..
  39. Ojima Kato T, Yamamoto N, Nagai S, Shima K, Akiyama Y, Ota J, et al. Application of proteotyping Strain Solution™ ver. 2 software and theoretically calculated mass database in MALDI-TOF MS typing of Salmonella serotype. Appl Microbiol Biotechnol. 2017;101:8557-8569 pubmed publisher
    ..L17, L21, L25, and S7, Mn-cofactor-containing superoxide dismutase (SodA), peptidyl-prolyl cis-trans isomerase C (PPIase C), and protein Gns, and uncharacterized proteins YibT, YaiA, and YciF, that can allow serotyping of Salmonella...
  40. Schiene Fischer C, Yu C. Receptor accessory folding helper enzymes: the functional role of peptidyl prolyl cis/trans isomerases. FEBS Lett. 2001;495:1-6 pubmed
    ..PPIases play a critical role in the functional arrangement of components within receptor heterocomplexes. ..
  41. Deivanayagam C, Carson M, Thotakura A, Narayana S, Chodavarapu R. Structure of FKBP12.6 in complex with rapamycin. Acta Crystallogr D Biol Crystallogr. 2000;56:266-71 pubmed
    ..6 toward the hydrophobic pocket. This displacement was not predicted by homology modeling studies. Analyses of the residues that are likely to confer the RyR2-binding specificity are presented. ..
  42. Wang G, Shen J, Sun J, Jiang Z, Fan J, Wang H, et al. Cyclophilin A Maintains Glioma-Initiating Cell Stemness by Regulating Wnt/β-Catenin Signaling. Clin Cancer Res. 2017;23:6640-6649 pubmed publisher
    ..Cyclophilin A (CypA) is a cytosolic protein that belongs to the peptidyl-prolyl isomerase (PPIase) family and the major intracellular target of the immunosuppressive drug cyclosporin A (CsA)...
  43. Marks A. Cellular functions of immunophilins. Physiol Rev. 1996;76:631-49 pubmed
    ..In each case, FKBPs modulate channel function possibly by enhancing the cooperativity between subunits...
  44. Dongsheng Z, Zhiguang F, Junfeng J, Zifan L, Li W. Cyclophilin A Aggravates Collagen-Induced Arthritis via Promoting Classically Activated Macrophages. Inflammation. 2017;: pubmed publisher
    ..activity of NF-κB, the pivotal transcriptional factor regulating M1 polarization, dependent of its PPIase activity...
  45. Rogals M, Greenwood A, Kwon J, Lu K, Nicholson L. Neighboring phosphoSer-Pro motifs in the undefined domain of IRAK1 impart bivalent advantage for Pin1 binding. FEBS J. 2016;283:4528-4548 pubmed publisher
    The peptidyl prolyl isomerase Pin1 has two domains that are considered to be its binding (WW) and catalytic (PPIase) domains, both of which interact with phosphorylated Ser/Thr-Pro motifs...
  46. Seufert F, Kuhn M, Hein M, Weiwad M, Vivoli M, Norville I, et al. Development, synthesis and structure-activity-relationships of inhibitors of the macrophage infectivity potentiator (Mip) proteins of Legionella pneumophila and Burkholderia pseudomallei. Bioorg Med Chem. 2016;24:5134-5147 pubmed publisher
    ..The Mip proteins of B. pseudomallei and L. pneumophila exhibit peptidyl-prolyl cis/trans isomerase (PPIase) activity and belong to the PPIase superfamily...
  47. Oh Y, Jeong K, Kim K, Lee Y, Jeong S, Kim S, et al. Cyclophilin B protects SH-SY5Y human neuroblastoma cells against MPP(+)-induced neurotoxicity via JNK pathway. Biochem Biophys Res Commun. 2016;478:1396-402 pubmed publisher
    ..CypB has peptidyl-prolyl cis-trans isomerase (PPIase) activity...
  48. Na T, Huang Z, Dai D, Zhang Y, Dai Y. Abrupt changes in FKBP12.6 and SERCA2a expression contribute to sudden occurrence of ventricular fibrillation on reperfusion and are prevented by CPU86017. Acta Pharmacol Sin. 2007;28:773-82 pubmed
    ..Abrupt changes in the expression of FKBP12.6, SERCA2a, PKA, and ECE on reperfusion against ischemia, which are responsible for the rapid occurrence of VF, have been observed. These changes are effectively prevented by CPU86017. ..
  49. Hunt D, Jones P, Wang R, Chen W, Bolstad J, Chen K, et al. K201 (JTV519) suppresses spontaneous Ca2+ release and [3H]ryanodine binding to RyR2 irrespective of FKBP12.6 association. Biochem J. 2007;404:431-8 pubmed
    ..Our results also suggest that suppression of spontaneous Ca2+ release and the activity of RyR2 contributes, at least in part, to the anti-arrhythmic properties of K201. ..
  50. Bultynck G, Rossi D, Callewaert G, Missiaen L, Sorrentino V, Parys J, et al. The conserved sites for the FK506-binding proteins in ryanodine receptors and inositol 1,4,5-trisphosphate receptors are structurally and functionally different. J Biol Chem. 2001;276:47715-24 pubmed
    ..Structural differences in the FKBP-binding site of RyRs and IP(3)Rs may contribute to the occurrence of a stable interaction between RyR isoforms and FKBPs and to the absence of such interaction with IP(3)Rs. ..
  51. Arié J, Sassoon N, Betton J. Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli. Mol Microbiol. 2001;39:199-210 pubmed
    ..Here, we show that FkpA, a heat shock periplasmic peptidyl-prolyl cis/trans isomerase (PPIase), suppresses the formation of inclusion bodies from a defective-folding variant of the maltose-binding protein, ..
  52. Holland E, Goldstone J, Pessah I, Whitehead A, Reid N, Karchner S, et al. Ryanodine receptor and FK506 binding protein 1 in the Atlantic killifish (Fundulus heteroclitus): A phylogenetic and population-based comparison. Aquat Toxicol. 2017;192:105-115 pubmed publisher
    ..6kDa (genes FKBP1A; FKBP1B), which promote NDL PCB-triggered Ca2+ dysregulation...
  53. Habib A, Karmali V, Polavarapu R, Akahori H, Cheng Q, Pachura K, et al. Sirolimus-FKBP12.6 impairs endothelial barrier function through protein kinase C-α activation and disruption of the p120-vascular endothelial cadherin interaction. Arterioscler Thromb Vasc Biol. 2013;33:2425-31 pubmed publisher
    ..These data suggest this mechanism may be an important contributor of SRL side effects related to impaired EBF. ..
  54. Lam E, Martin M, Timerman A, Sabers C, Fleischer S, Lukas T, et al. A novel FK506 binding protein can mediate the immunosuppressive effects of FK506 and is associated with the cardiac ryanodine receptor. J Biol Chem. 1995;270:26511-22 pubmed
    ..Our results suggest that FKBP12.6 has both a unique physiological role in excitation-contraction coupling in cardiac muscle and the potential to contribute to the immunosuppressive and toxic effects of FK506 and rapamycin. ..