FKBP8 Antibody, FITC conjugated

1. Cycling between the inactive GDP- and the active GTP-bound state modulates the backbone dynamics of a C-terminal truncated form, RhebDeltaCT, which is suggested to influence its interactions. We further investigated the interactions between RhebDeltaCT and the proposed Rheb-binding domain of the regulatory protein FKBP38. PMID: 29194576
2. Regulation of CLC-1 chloride channel biosynthesis by FKBP8 and Hsp90beta as a molecular model for myotonia congenita has been described. PMID: 27580824
3. Co-expression of FKBP8 with LC3A profoundly induces Parkin-independent mitophagy. Strikingly, even when acting as a mitophagy receptor, FKBP8 avoids degradation by escaping from mitochondria. In summary, this study identifies novel roles for FKBP8 and LC3A, which act together to induce mitophagy. PMID: 28381481
4. FKBP8 binding to Hsp90 did not substantially influence its ATPase activity PMID: 28278223
5. The information presented here provides important clues for understanding the catalytic activity of FKBP38, its regulation by the unique N-terminal extension, and the potential calcium- and calmodulin-mediated activation of FKBP38. PMID: 24145868
6. Overexpression of permanently active S100P in Huh-7 cells inhibited the interaction of FKBP38 with Bcl-2, resulting in the suppression of Bcl-2 stability PMID: 24295050
7. FK506 binding protein 8 peptidylprolyl isomerase activity manages a late stage of cystic fibrosis transmembrane conductance regulator (CFTR) folding and stability PMID: 22474283
8. The derived structure model of the complex between Bcl-2 and the FKBP38 catalytic domain features both electrostatic and hydrophobic intermolecular contacts and provides a rationale for the regulation of the FKBP38/Bcl-2 interaction by Ca(2+). PMID: 22523079
9. Data support a dual role for FKBP38 in regulating CFTR synthesis and post-translational folding. PMID: 22030396
10. a dual mechanism for PA activation of mTORC1: PA displaces FKBP38 from mTOR and allosterically stimulates the catalytic activity of mTORC1. PMID: 21737445
11. this charge-sensitive site in the FKBP domain participates in the regulation of FKBP38 function by enabling electrostatic interactions with ligand proteins and/or salt ions such as Ca(2+) PMID: 20140889
12. novel insights into the structural arrangement of FKBP38/calmodulin complex PMID: 20707607
13. FKBP38 is a key player in regulating the function of Bcl-2 by antagonizing caspase-dependent degradation through the direct interaction with the flexible loop domain of Bcl-2, which contains the caspase cleavage site PMID: 20139069
14. Rheb GTPase controls apoptosis by regulating interaction of FKBP38 with Bcl-2 and Bcl-XL PMID: 20048149
15. FKBP38 plays a role in TSC gene-dependent cell size regulation. PMID: 12894220
16. Bcl-2 interacts with FKBP38 through the unstructured loop, and the interaction appears to regulate phosphorylation in the loop of Bcl-2 PMID: 15733859
17. FKBP38 indirectly affects the subcellular distribution of calcineurin by interaction with typical calcineurin ligands, as exemplified by the anti-apoptotic protein Bcl-2. PMID: 15757646
18. Molecular model of the FK506-binding domain of FKBP38. PMID: 16604427
19. the complex consisting of NS5A, FKBP8, and Hsp90 plays an important role in HCV RNA replication PMID: 17024179
20. Data suggest that the peptidyl prolyl cis/trans isomerase FKBP38 determines hypoxia-inducible transcription factor prolyl-4-hydroxylase PHD2 protein stability. PMID: 17353276
21. FKBP38 is a co-chaperone of HERG and contributes via the Hsc70/Hsp90 chaperone system to the trafficking of wild type and mutant HERG potassium channels PMID: 17569659
22. FKBP38 functions to anchor the 26S proteasome at the organellar membrane PMID: 17573772
23. interaction between the catalytic FKBP38 domain and the N-terminal CaM domain activates FKBP38 and, as a consequence, also regulates Bcl-2. PMID: 17942410
24. findings suggest that FKBP38 is an endogenous inhibitor of mTOR, whose inhibitory activity is antagonized by Rheb in response to growth factor stimulation and nutrient availability PMID: 17991864
25. These results suggest that specific interaction of NS5A with FKBP8 in the cytoplasmic compartment plays a crucial role in the replication of HCV. PMID: 18216108
26. FKBP38 is a bona fide effector of Rheb and the ability to interact with FKBP38 is important for Rheb as an activator of mTOR PMID: 18658153
27. neither TCTP nor FKBP38 regulates mTORC1 signaling. PMID: 18676370
28. FKBP38 plays only a very minor, if any, role in mTORC1 activation. PMID: 19222999
29. Data indicate that PHD2 protein stability is regulated by a ubiquitin-independent proteasomal pathway involving FKBP38 as adaptor protein that mediates proteasomal interaction. PMID: 19546213

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HGNC: 3724

OMIM: 604840

KEGG: hsa:23770

STRING: 9606.ENSP00000222308

UniGene: Hs.173464