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FKBP8  -  FK506 binding protein 8, 38kDa

Homo sapiens

Synonyms: 38 kDa FK506-binding protein, 38 kDa FKBP, FK506-binding protein 8, FKBP-38, FKBP-8, ...
 
 
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Disease relevance of FKBP8

  • The specific FKBP38 inhibitor N-(N',N'-dimethylcarboxamidomethyl)cycloheximide has potent neuroprotective and neurotrophic properties in brain ischemia [1].
  • Thus, our results demonstrate that FKBP38 inhibition by DM-CHX regulates neuronal cell death and proliferation, providing a promising strategy for the treatment of acute and/or chronic neurodegenerative diseases [1].
  • In the context of the high expression of FKBP38 in neuroblastoma cells, these data suggest that FKBP38.CaM/Ca(2+) inhibition can mediate neurotrophic properties of FKBP ligands [1].
  • The siRNA-mediated knockdown of FKBP8 in a human hepatoma cell line harboring an HCV RNA replicon suppressed HCV RNA replication, and this reduction was reversed by the expression of an siRNA-resistant FKBP8 mutant [2].
  • Hepatitis C virus RNA replication is regulated by FKBP8 and Hsp90 [2].
 

High impact information on FKBP8

  • Overexpression of FKBP38 blocks apoptosis, whereas functional inhibition of this protein by a dominant-negative mutant or by RNA interference promotes apoptosis [3].
  • Here we show that mitochondrial FK506-binding protein 38 (FKBP38), unlike FKBP12, binds to and inhibits calcineurin in the absence of the immunosuppressant FK506, suggesting that FKBP38 is an inherent inhibitor of this phosphatase [3].
  • FKBP38 is associated with Bcl-2 and Bcl-x(L) in immunoprecipitation assays and colocalizes with these proteins in mitochondria; in addition, the expression of FKBP38 mutant proteins induces a marked redistribution of Bcl-2 and Bcl-x(L) [3].
  • Association between Bcl-2 and the active site of Ca2+/calmodulin/FKBP38 regulates Bcl-2 function and thereby participates in the promotion of apoptosis in neuronal tissues [4].
  • Here, we demonstrate that FKBP38, an immunophilin family member residing in the mitochondrial membrane, is an authentic PS1/2-interacting protein [5].
 

Chemical compound and disease context of FKBP8

 

Biological context of FKBP8

  • Although it is expressed broadly, FKBP8 is required to antagonize SHH signaling primarily in neural tissues, suggesting that hedgehog signal transduction is subject to cell-type specific modulation during mammalian development [6].
  • The immunophilin homolog FKBP8 has been implicated in the regulation of apoptosis [7].
  • The extended FKBP8 ORFs are 46 and 44 kDa in mouse and 45 kDa in human [7].
  • The flexible loop of Bcl-2 is required for molecular interaction with immunosuppressant FK-506 binding protein 38 (FKBP38) [8].
  • Here, we investigated the molecular interaction between FKBP38 and Bcl-2, and demonstrated that Bcl-2 interacts with FKBP38 through the unstructured loop, and the interaction appears to regulate phosphorylation in the loop of Bcl-2 [8].
 

Anatomical context of FKBP8

 

Associations of FKBP8 with chemical compounds

  • Additionally, we examined the role of the Bcl-2 BH4 domain in mediating binding to FKBP38, the Bcl-2 mitochondrial chaperone [11].
  • Backbone (1)H, (13)C, and (15)N resonance assignments of the N-terminal domain of FKBP38 (FKBP38NTD) [12].
 

Other interactions of FKBP8

  • In addition, FKBPr38 contains a consensus leucine-zipper repeat [13].
  • Our results suggest that FKBP38 appears to show chaperone activities in the citrate synthase aggregation assays during thermal denaturation and affect solubility of Bcl-2 when they are co-expressed [14].
 

Analytical, diagnostic and therapeutic context of FKBP8

References

  1. The specific FKBP38 inhibitor N-(N',N'-dimethylcarboxamidomethyl)cycloheximide has potent neuroprotective and neurotrophic properties in brain ischemia. Edlich, F., Weiwad, M., Wildemann, D., Jarczowski, F., Kilka, S., Moutty, M.C., Jahreis, G., Lücke, C., Schmidt, W., Striggow, F., Fischer, G. J. Biol. Chem. (2006) [Pubmed]
  2. Hepatitis C virus RNA replication is regulated by FKBP8 and Hsp90. Okamoto, T., Nishimura, Y., Ichimura, T., Suzuki, K., Miyamura, T., Suzuki, T., Moriishi, K., Matsuura, Y. EMBO J. (2006) [Pubmed]
  3. Inherent calcineurin inhibitor FKBP38 targets Bcl-2 to mitochondria and inhibits apoptosis. Shirane, M., Nakayama, K.I. Nat. Cell Biol. (2003) [Pubmed]
  4. Bcl-2 regulator FKBP38 is activated by Ca2+/calmodulin. Edlich, F., Weiwad, M., Erdmann, F., Fanghänel, J., Jarczowski, F., Rahfeld, J.U., Fischer, G. EMBO J. (2005) [Pubmed]
  5. Interaction of presenilins with FKBP38 promotes apoptosis by reducing mitochondrial Bcl-2. Wang, H.Q., Nakaya, Y., Du, Z., Yamane, T., Shirane, M., Kudo, T., Takeda, M., Takebayashi, K., Noda, Y., Nakayama, K.I., Nishimura, M. Hum. Mol. Genet. (2005) [Pubmed]
  6. FKBP8 is a negative regulator of mouse sonic hedgehog signaling in neural tissues. Bulgakov, O.V., Eggenschwiler, J.T., Hong, D.H., Anderson, K.V., Li, T. Development (2004) [Pubmed]
  7. Fkbp8: novel isoforms, genomic organization, and characterization of a forebrain promoter in transgenic mice. Nielsen, J.V., Mitchelmore, C., Pedersen, K.M., Kjaerulff, K.M., Finsen, B., Jensen, N.A. Genomics (2004) [Pubmed]
  8. The flexible loop of Bcl-2 is required for molecular interaction with immunosuppressant FK-506 binding protein 38 (FKBP38). Kang, C.B., Tai, J., Chia, J., Yoon, H.S. FEBS Lett. (2005) [Pubmed]
  9. Hepatitis C virus non-structural protein NS5A interacts with FKBP38 and inhibits apoptosis in Huh7 hepatoma cells. Wang, J., Tong, W., Zhang, X., Chen, L., Yi, Z., Pan, T., Hu, Y., Xiang, L., Yuan, Z. FEBS Lett. (2006) [Pubmed]
  10. Comparative proteomic analysis of peripheral blood eosinophils from healthy donors and atopic dermatitis patients with eosinophilia. Yoon, S.W., Kim, T.Y., Sung, M.H., Kim, C.J., Poo, H. Proteomics (2005) [Pubmed]
  11. Bcl-2 localized at the nuclear compartment induces apoptosis after transient overexpression. Portier, B.P., Taglialatela, G. J. Biol. Chem. (2006) [Pubmed]
  12. Backbone (1)H, (13)C, and (15)N resonance assignments of the N-terminal domain of FKBP38 (FKBP38NTD). Kang, C.B., Ye, H., Vivekanandan, S., Simon, B., Sattler, M., Yoon, H.S. J. Biomol. NMR (2006) [Pubmed]
  13. Isolation of a cDNA encoding a novel human FK506-binding protein homolog containing leucine zipper and tetratricopeptide repeat motifs. Lam, E., Martin, M., Wiederrecht, G. Gene (1995) [Pubmed]
  14. Molecular characterization of FK-506 binding protein 38 and its potential regulatory role on the anti-apoptotic protein Bcl-2. Kang, C.B., Feng, L., Chia, J., Yoon, H.S. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
 
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