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Our findings thus indicate that the FKBP38-ANKMY2 (Montrer ANKMY2 Anticorps) axis plays a key role in regulation of Shh (Montrer SHH Anticorps) signaling in vivo.
In pre-hearing time Fkbp8-specific signal was also observed in the tectorial membrane, whose alpha- and beta-Tectorin (Montrer TECTB Anticorps) 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 (Montrer FKBP1A Anticorps).
Results show that FKBP8 is an essential antagonist of sonic hedgehog (Montrer SHH Anticorps) signaling in central nervous system development.
FKBP38 functions to anchor the 26S proteasome (Montrer Psmd4 Anticorps) 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 (Montrer SHH Anticorps) signaling pathway cell-autonomously dependent on the Gli2 (Montrer GLI2 Anticorps) transcription factor and kinesin-2 (Montrer KIF2A Anticorps) subunit Kif3a (Montrer KIF3A Anticorps), a component of the intraflagellar transport machinery used to generate cilia.
Data indicate that PHD2 (Montrer EGLN1 Anticorps) protein stability is regulated by a ubiquitin-independent proteasomal pathway involving FKBP38 as adaptor protein that mediates proteasomal interaction.
Regulation of CLC-1 (Montrer CLCN1 Anticorps) chloride channel (Montrer CLCA1 Anticorps) biosynthesis by FKBP8 and Hsp90beta (Montrer HSP90AB1 Anticorps) as a molecular model for myotonia congenita has been described.
Co-expression of FKBP8 with LC3A (Montrer MAP1LC3A Anticorps) profoundly induces Parkin (Montrer PARK2 Anticorps)-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 (Montrer MAP1LC3A Anticorps), which act together to induce mitophagy.
FKBP8 binding to Hsp90 (Montrer HSP90 Anticorps) did not substantially influence its ATPase (Montrer DNAH8 Anticorps) 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 (Montrer S100P Anticorps) in Huh-7 cells inhibited the interaction of FKBP38 with Bcl-2 (Montrer BCL2 Anticorps), resulting in the suppression of Bcl-2 (Montrer BCL2 Anticorps) stability
FK506 binding protein 8 peptidylprolyl isomerase activity manages a late stage of cystic fibrosis transmembrane conductance regulator (CFTR (Montrer CFTR Anticorps)) folding and stability
The derived structure model of the complex between Bcl-2 (Montrer BCL2 Anticorps) and the FKBP38 catalytic domain features both electrostatic and hydrophobic intermolecular contacts and provides a rationale for the regulation of the FKBP38/Bcl-2 (Montrer BCL2 Anticorps) interaction by Ca(2 (Montrer CA2 Anticorps)+).
Data support a dual role for FKBP38 in regulating CFTR (Montrer CFTR Anticorps) synthesis and post-translational folding.
a dual mechanism for PA activation of mTORC1: PA displaces FKBP38 from mTOR (Montrer FRAP1 Anticorps) and allosterically stimulates the catalytic activity of mTORC1.
this charge-sensitive site in the FKBP (Montrer FKBP7 Anticorps) domain participates in the regulation of FKBP38 function by enabling electrostatic interactions with ligand proteins and/or salt ions such as Ca(2 (Montrer CA2 Anticorps)+)
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)