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FKBP1B  -  FK506 binding protein 1B, 12.6 kDa

Homo sapiens

Synonyms: 12.6 kDa FK506-binding protein, 12.6 kDa FKBP, FK506-binding protein 1B, FKBP-12.6, FKBP-1B, ...
 
 
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Disease relevance of FKBP1B

  • Dysregulated ryanodine receptors mediate cellular toxicity: restoration of normal phenotype by FKBP12.6 [1].
  • A novel mutation in FKBP12.6 binding region of the human cardiac ryanodine receptor gene (R2401H) in a Japanese patient with catecholaminergic polymorphic ventricular tachycardia [2].
  • The inotropic adaptation during late preconditioning against myocardial stunning is associated with an increase in FKBP12.6 [3].
  • Macrophage infectivity potentiator (CbMip, 23.5 kDa) protein of the obligate intracellular bacterium, Coxiella burnetii, was shown previously to belong to the family of FKBPs based on sequence homology and peptidyl-prolyl cis/trans isomerase (PPIase) activity [4].
  • A thorough understanding of the structural basis of RyR2-FKBP12.6 interaction should aid in understanding the roles that have been proposed for FKBP12.6 in heart failure and in certain forms of sudden cardiac death [5].
 

High impact information on FKBP1B

  • We show that protein kinase A (PKA) phosphorylation of RyR2 dissociates FKBP12.6 and regulates the channel open probability (Po) [6].
  • PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts [6].
  • The first 38 amino-acid residues of porcine PPIase and of bovine cyclophilin are identical and the two proteins both have a relative molecular mass of about 17,000 (ref. 7). The catalysis of prolyl isomerization in oligopeptides and of protein folding by PPIase are strongly inhibited in the presence of low levels of CsA [7].
  • Pin1 is a novel essential peptidyl-prolyl isomerase (PPIase) that inhibits entry into mitosis and is also required for proper progression through mitosis, but its substrate(s) and function(s) remain to be determined [8].
  • Peptidyl prolyl cis-trans isomerase activity (PPIase) was measured in SF from knee punctures of 26 patients with RA and five patients with knee osteoarthritis (OA) [9].
 

Chemical compound and disease context of FKBP1B

  • In addition, a variety of k(cat)/K(m) values, ranging from 1.1 mM(-1) s(-1) for the B. subtilis PPIase to over 10 mM(-1) s(-1) for human and 13 mM(-1) s(-1) for E. coli, were detected using the common substrate suc-Ala-Ala-Pro-Phe-pNA [10].
 

Biological context of FKBP1B

 

Anatomical context of FKBP1B

 

Associations of FKBP1B with chemical compounds

  • However, in CHO(hRyR2) cells co-expressing FKBP12.6, Ca(2+) release triggered by the addition of 4-chloro- m -cresol was markedly decreased [16].
  • Expression of eGFP-tagged RyR constructs encoding distinct transmembrane topological models profoundly altered intracellular Ca(2+) handling and was refractory to modulation by ryanodine, FKBP12.6 and caffeine [17].
  • In contrast to the wild-type enzyme, several variants of FKBP12 with greatly reduced PPIase activity were unable to suppress EGF receptor tyrosine kinase significantly [18].
  • The proline residue in PPIase substrates at the P1' subsite, which follows the isomerizing peptide bond, appears to be the common recognition element for all subfamilies of this enzyme class [19].
  • Generally, PPIase catalysis demonstrated stereospecificity for monofluoro substitutions at the 4-position of the pyrrolidine ring [19].
 

Physical interactions of FKBP1B

  • 6. However, expression of a large RyR2 C-terminal construct in mammalian cells encompassing the pore-forming transmembrane domains exhibits rapamycin-sensitive binding specifically to FKBP12.6 but not to FKBP12 [20].
  • We also found that a distinct, alternatively spliced variant of FKBP12.6 was unable to interact with RyR [21].
 

Regulatory relationships of FKBP1B

  • PKA phosphorylation of RyR2 induces dissociation of the regulatory protein FKBP12.6 resulting in channels with increased sensitivity to Ca2+-induced Ca2+ release [22].
 

Other interactions of FKBP1B

  • Our studies suggest that a novel interaction site for FKBP12.6 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 [20].
  • Interaction of FKBP12.6 with the cardiac ryanodine receptor C-terminal domain [20].
  • RyR2 channels form large complexes with additional regulatory proteins, including FKBP12.6 and calsequestrin 2 (CASQ2) [23].
  • After 4-week treatment, CPU0213 was capable to attenuate completely the down-regulated FKBP12.6 and SERCA2a, and up-regulated ET system in association with a recovery of the cardiac insufficiency of diabetic cardiomyopathy [24].
  • This review discusses the regulation of RyRs by FKBPs and the possibility that defective modulation of RyR2 by FKBP12.6 could play a role in heart failure, CPVT, and ARVD2 [25].
 

Analytical, diagnostic and therapeutic context of FKBP1B

References

  1. Dysregulated ryanodine receptors mediate cellular toxicity: restoration of normal phenotype by FKBP12.6. George, C.H., Higgs, G.V., Mackrill, J.J., Lai, F.A. J. Biol. Chem. (2003) [Pubmed]
  2. A novel mutation in FKBP12.6 binding region of the human cardiac ryanodine receptor gene (R2401H) in a Japanese patient with catecholaminergic polymorphic ventricular tachycardia. Aizawa, Y., Ueda, K., Komura, S., Washizuka, T., Chinushi, M., Inagaki, N., Matsumoto, Y., Hayashi, T., Takahashi, M., Nakano, N., Yasunami, M., Kimura, A., Hiraoka, M., Aizawa, Y. International journal of cardiology. (2005) [Pubmed]
  3. The inotropic adaptation during late preconditioning against myocardial stunning is associated with an increase in FKBP12.6. Lucats, L., Vinet, L., Bizé, A., Monnet, X., Morin, D., Su, J.B., Rouet-Benzineb, P., Cazorla, O., Mercadier, J.J., Hittinger, L., Berdeaux, A., Ghaleh, B. Cardiovasc. Res. (2007) [Pubmed]
  4. Synthesis in Escherichia coli of two smaller enzymically active analogues of Coxiella burnetii macrophage infectivity potentiator (CbMip) protein utilizing a single open reading frame from the cbmip gene. Mo, Y.Y., Seshu, J., Wang, D., Mallavia, L.P. Biochem. J. (1998) [Pubmed]
  5. Three-dimensional visualization of FKBP12.6 binding to an open conformation of cardiac ryanodine receptor. Sharma, M.R., Jeyakumar, L.H., Fleischer, S., Wagenknecht, T. Biophys. J. (2006) [Pubmed]
  6. PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts. Marx, S.O., Reiken, S., Hisamatsu, Y., Jayaraman, T., Burkhoff, D., Rosemblit, N., Marks, A.R. Cell (2000) [Pubmed]
  7. Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins. Fischer, G., Wittmann-Liebold, B., Lang, K., Kiefhaber, T., Schmid, F.X. Nature (1989) [Pubmed]
  8. The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins. Shen, M., Stukenberg, P.T., Kirschner, M.W., Lu, K.P. Genes Dev. (1998) [Pubmed]
  9. Presence of cyclophilin A in synovial fluids of patients with rheumatoid arthritis. Billich, A., Winkler, G., Aschauer, H., Rot, A., Peichl, P. J. Exp. Med. (1997) [Pubmed]
  10. Peptidyl-prolyl cis-trans isomerase of Bacillus subtilis: identification of residues involved in cyclosporin A affinity and catalytic efficiency. Göthel, S.F., Herrler, M., Marahiel, M.A. Biochemistry (1996) [Pubmed]
  11. Evidence of association between FKBP1B and thyroid autoimmune disorders in a large Tunisian family. Maalej, A., Mbarki, F., Rebai, A., Karray, F., Jouida, J., Abid, M., Ayadi, H. Autoimmunity (2004) [Pubmed]
  12. 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). Masumiya, H., Wang, R., Zhang, J., Xiao, B., Chen, S.R. J. Biol. Chem. (2003) [Pubmed]
  13. A novel FK506 binding protein can mediate the immunosuppressive effects of FK506 and is associated with the cardiac ryanodine receptor. Lam, E., Martin, M.M., Timerman, A.P., Sabers, C., Fleischer, S., Lukas, T., Abraham, R.T., O'Keefe, S.J., O'Neill, E.A., Wiederrecht, G.J. J. Biol. Chem. (1995) [Pubmed]
  14. Cyclic ADP-ribose binds to FK506-binding protein 12.6 to release Ca2+ from islet microsomes. Noguchi, N., Takasawa, S., Nata, K., Tohgo, A., Kato, I., Ikehata, F., Yonekura, H., Okamoto, H. J. Biol. Chem. (1997) [Pubmed]
  15. FK506 does not affect cardiac contractility and adrenergic response in vitro. Milting, H., Janssen, P.M., Wangemann, T., Kögler, H., Domeier, E., Seidler, T., Hakim, K., Grapow, M., Zeitz, O., Prestle, J., Zerkowski, H.R. Eur. J. Pharmacol. (2001) [Pubmed]
  16. In situ modulation of the human cardiac ryanodine receptor (hRyR2) by FKBP12.6. George, C.H., Sorathia, R., Bertrand, B.M., Lai, F.A. Biochem. J. (2003) [Pubmed]
  17. Ryanodine receptor regulation by intramolecular interaction between cytoplasmic and transmembrane domains. George, C.H., Jundi, H., Thomas, N.L., Scoote, M., Walters, N., Williams, A.J., Lai, F.A. Mol. Biol. Cell (2004) [Pubmed]
  18. Effects of FK506-binding protein 12 and FK506 on autophosphorylation of epidermal growth factor receptor. Lopez-Ilasaca, M., Schiene, C., Küllertz, G., Tradler, T., Fischer, G., Wetzker, R. J. Biol. Chem. (1998) [Pubmed]
  19. Peptidyl prolyl cis/trans-isomerases: comparative reactivities of cyclophilins, FK506-binding proteins, and parvulins with fluorinated oligopeptide and protein substrates. Golbik, R., Yu, C., Weyher-Stingl, E., Huber, R., Moroder, L., Budisa, N., Schiene-Fischer, C. Biochemistry (2005) [Pubmed]
  20. Interaction of FKBP12.6 with the cardiac ryanodine receptor C-terminal domain. Zissimopoulos, S., Lai, F.A. J. Biol. Chem. (2005) [Pubmed]
  21. Central domain of the human cardiac muscle ryanodine receptor does not mediate interaction with FKBP12.6. Zissimopoulos, S., Lai, F.A. Cell Biochem. Biophys. (2005) [Pubmed]
  22. Ryanodine receptors, FKBP12, and heart failure. Marks, A.R. Front. Biosci. (2002) [Pubmed]
  23. Catecholaminergic polymorphic ventricular tachycardia: recent mechanistic insights. Kontula, K., Laitinen, P.J., Lehtonen, A., Toivonen, L., Viitasalo, M., Swan, H. Cardiovasc. Res. (2005) [Pubmed]
  24. A novel endothelin receptor antagonist CPU0213 improves diabetic cardiac insufficiency attributed to up-regulation of the expression of FKBP12.6, SERCA2a, and PLB in rats. Qi, M.Y., Xia, H.J., Dai, D.Z., Dai, Y. J. Cardiovasc. Pharmacol. (2006) [Pubmed]
  25. Regulation of ryanodine receptors by FK506 binding proteins. Chelu, M.G., Danila, C.I., Gilman, C.P., Hamilton, S.L. Trends Cardiovasc. Med. (2004) [Pubmed]
  26. Three-dimensional localization of divergent region 3 of the ryanodine receptor to the clamp-shaped structures adjacent to the FKBP binding sites. Zhang, J., Liu, Z., Masumiya, H., Wang, R., Jiang, D., Li, F., Wagenknecht, T., Chen, S.R. J. Biol. Chem. (2003) [Pubmed]
  27. Genomic organization, chromosomal localization, and promoter of human gene for FK506-binding protein 12.6. Nakazawa, T., Takasawa, S., Noguchi, N., Nata, K., Tohgo, A., Mori, M., Nakagawara, K., Akiyama, T., Ikeda, T., Yamauchi, A., Takahashi, I., Yoshikawa, T., Okamoto, H. Gene (2005) [Pubmed]
  28. Molecular cloning and expression of a novel human gene that is highly homologous to human FK506-binding protein 12kDa (hFKBP-12) and characterization of two alternatively spliced transcripts. Arakawa, H., Nagase, H., Hayashi, N., Fujiwara, T., Ogawa, M., Shin, S., Nakamura, Y. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
  29. Biochemical and functional analyses of the Mip protein: influence of the N-terminal half and of peptidylprolyl isomerase activity on the virulence of Legionella pneumophila. Köhler, R., Fanghänel, J., König, B., Lüneberg, E., Frosch, M., Rahfeld, J.U., Hilgenfeld, R., Fischer, G., Hacker, J., Steinert, M. Infect. Immun. (2003) [Pubmed]
 
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