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Human FKBP8 Protein expressed in Wheat germ - ABIN1354140
Ardi, Alexander, Johnson, McAlpine: Macrocycles that inhibit the binding between heat shock protein 90 and TPR-containing proteins. in ACS chemical biology 2011
Our findings thus indicate that the FKBP38-ANKMY2 (show ANKMY2 Proteins) axis plays a key role in regulation of Shh (show SHH Proteins) signaling in vivo.
In pre-hearing time Fkbp8-specific signal was also observed in the tectorial membrane, whose alpha- and beta-Tectorin (show TECTB Proteins) 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 Proteins).
Results show that FKBP8 is an essential antagonist of sonic hedgehog (show SHH Proteins) signaling in central nervous system development.
FKBP38 functions to anchor the 26S proteasome (show Psmd4 Proteins) 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 Proteins) signaling pathway cell-autonomously dependent on the Gli2 transcription factor and kinesin-2 (show KIF2A Proteins) subunit Kif3a (show KIF3A Proteins), a component of the intraflagellar transport machinery used to generate cilia.
Data indicate that PHD2 (show EGLN1 Proteins) protein stability is regulated by a ubiquitin-independent proteasomal pathway involving FKBP38 as adaptor protein that mediates proteasomal interaction.
FKBP8 binding to Hsp90 did not substantially influence its ATPase 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 (show CALM1 Proteins)-mediated activation of FKBP38.
Overexpression of permanently active S100P (show S100P Proteins) in Huh-7 cells inhibited the interaction of FKBP38 with Bcl-2 (show BCL2 Proteins), resulting in the suppression of Bcl-2 (show BCL2 Proteins) stability
FK506 binding protein 8 peptidylprolyl isomerase activity manages a late stage of cystic fibrosis transmembrane conductance regulator (CFTR (show CFTR Proteins)) folding and stability
The derived structure model of the complex between Bcl-2 (show BCL2 Proteins) 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 Proteins) interaction by Ca(2 (show CA2 Proteins)+).
Data support a dual role for FKBP38 in regulating CFTR (show CFTR Proteins) synthesis and post-translational folding.
a dual mechanism for PA activation of mTORC1: PA displaces FKBP38 from mTOR (show FRAP1 Proteins) and allosterically stimulates the catalytic activity of mTORC1.
this charge-sensitive site in the FKBP (show FKBP7 Proteins) 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 Proteins)+)
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.
novel insights into the structural arrangement of FKBP38/calmodulin (show CALM1 Proteins) complex
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)