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FKBP8 Enhances Protein Stability of the CLC-1 Chloride Channel at the Plasma Membrane
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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.
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Regulation of CLC-1 chloride channel biosynthesis by FKBP8 and Hsp90beta as a molecular model for myotonia congenita has been described.
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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.
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FKBP8 binding to Hsp90 did not substantially influence its ATPase activity
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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.
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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
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FK506 binding protein 8 peptidylprolyl isomerase activity manages a late stage of cystic fibrosis transmembrane conductance regulator (CFTR) folding and stability
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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+).
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Data support a dual role for FKBP38 in regulating CFTR synthesis and post-translational folding.
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a dual mechanism for PA activation of mTORC1: PA displaces FKBP38 from mTOR and allosterically stimulates the catalytic activity of mTORC1.
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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+)
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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.
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novel insights into the structural arrangement of FKBP38/calmodulin complex
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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
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Rheb GTPase controls apoptosis by regulating interaction of FKBP38 with Bcl-2 and Bcl-XL
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FKBP38 plays a role in TSC gene-dependent cell size regulation.
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Bcl-2 interacts with FKBP38 through the unstructured loop, and the interaction appears to regulate phosphorylation in the loop of Bcl-2
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FKBP38 indirectly affects the subcellular distribution of calcineurin by interaction with typical calcineurin ligands, as exemplified by the anti-apoptotic protein Bcl-2.
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Molecular model of the FK506-binding domain of FKBP38.
