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Our findings thus indicate that the FKBP38-ANKMY2 (show ANKMY2 Antibodies) axis plays a key role in regulation of Shh (show SHH Antibodies) signaling in vivo.
In pre-hearing time Fkbp8-specific signal was also observed in the tectorial membrane, whose alpha- and beta-Tectorin (show TECTB Antibodies) components show similar time-dependent expression of mRNA as Fkbp8.
used systemic gene transfer in tumor-bearing mice to identify novel antiinvasive and antimetastatic functions for Fkbp8, and subsequently for Fkbp1a (show FKBP1A Antibodies).
Results show that FKBP8 is an essential antagonist of sonic hedgehog (show SHH Antibodies) signaling in central nervous system development.
FKBP38 functions to anchor the 26S proteasome (show Psmd4 Antibodies) at the organellar membrane
Gene expression analysis of Fkbp8 mutants revealed a perturbation of expression of neural tube patterning genes, suggesting that endogenous FKBP8 activity establishes dorso-ventral patterning of the neural tube.
Findings suggest that FKBP38 is required for neuroectodermal organization during neural tube formation as a result of its anti-apoptotic activity and regulation of neurite extension
Disruption of FKBP8 function activates the Shh (show SHH Antibodies) signaling pathway cell-autonomously dependent on the Gli2 (show GLI2 Antibodies) transcription factor and kinesin-2 (show KIF2A Antibodies) subunit Kif3a (show KIF3A Antibodies), a component of the intraflagellar transport machinery used to generate cilia.
Data indicate that PHD2 (show EGLN1 Antibodies) protein stability is regulated by a ubiquitin-independent proteasomal pathway involving FKBP38 as adaptor protein that mediates proteasomal interaction.
Co-expression of FKBP8 with LC3A (show MAP1LC3A Antibodies) profoundly induces Parkin (show PARK2 Antibodies)-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 (show MAP1LC3A Antibodies), which act together to induce mitophagy.
FKBP8 binding to Hsp90 (show HSP90 Antibodies) did not substantially influence its ATPase (show DNAH8 Antibodies) activity
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.
Overexpression of permanently active S100P (show S100P Antibodies) in Huh-7 cells inhibited the interaction of FKBP38 with Bcl-2 (show BCL2 Antibodies), resulting in the suppression of Bcl-2 (show BCL2 Antibodies) stability
FK506 binding protein 8 peptidylprolyl isomerase activity manages a late stage of cystic fibrosis transmembrane conductance regulator (CFTR (show CFTR Antibodies)) folding and stability
The derived structure model of the complex between Bcl-2 (show BCL2 Antibodies) and the FKBP38 catalytic domain features both electrostatic and hydrophobic intermolecular contacts and provides a rationale for the regulation of the FKBP38/Bcl-2 (show BCL2 Antibodies) interaction by Ca(2 (show CA2 Antibodies)+).
Data support a dual role for FKBP38 in regulating CFTR (show CFTR Antibodies) synthesis and post-translational folding.
a dual mechanism for PA activation of mTORC1: PA displaces FKBP38 from mTOR (show FRAP1 Antibodies) and allosterically stimulates the catalytic activity of mTORC1.
this charge-sensitive site in the FKBP (show FKBP7 Antibodies) domain participates in the regulation of FKBP38 function by enabling electrostatic interactions with ligand proteins and/or salt ions such as Ca(2 (show CA2 Antibodies)+)
These results demonstrate that FKBP38 is a novel regulator of the oncogenic protein PRL-3 abundance and that alteration in the stability of PRL-3 can have a dramatic impact on cell proliferation.
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. Unlike the other members of the family, this encoded protein does not seem to have PPIase/rotamase activity. It may have a role in neurons associated with memory function.
peptidyl-prolyl cis-trans isomerase FKBP8
, FK506 binding protein 8, 38kDa
, peptidyl-prolyl cis-trans isomerase FKBP8-like
, FK506-binding protein 8
, 38 kDa FK506-binding protein
, 38 kDa FKBP
, FK506-binding protein 38
, PPIase FKBP8
, FK506-binding protein 8 (38kD)