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- W62803312 abstract "Research Article15 December 1994free access Immunophilins interact with calcineurin in the absence of exogenous immunosuppressive ligands. M.E. Cardenas M.E. Cardenas Department of Genetics, Duke University Medical Center, Durham, NC 27710. Search for more papers by this author C. Hemenway C. Hemenway Department of Genetics, Duke University Medical Center, Durham, NC 27710. Search for more papers by this author R.S. Muir R.S. Muir Department of Genetics, Duke University Medical Center, Durham, NC 27710. Search for more papers by this author R. Ye R. Ye Department of Genetics, Duke University Medical Center, Durham, NC 27710. Search for more papers by this author D. Fiorentino D. Fiorentino Department of Genetics, Duke University Medical Center, Durham, NC 27710. Search for more papers by this author J. Heitman J. Heitman Department of Genetics, Duke University Medical Center, Durham, NC 27710. Search for more papers by this author M.E. Cardenas M.E. Cardenas Department of Genetics, Duke University Medical Center, Durham, NC 27710. Search for more papers by this author C. Hemenway C. Hemenway Department of Genetics, Duke University Medical Center, Durham, NC 27710. Search for more papers by this author R.S. Muir R.S. Muir Department of Genetics, Duke University Medical Center, Durham, NC 27710. Search for more papers by this author R. Ye R. Ye Department of Genetics, Duke University Medical Center, Durham, NC 27710. Search for more papers by this author D. Fiorentino D. Fiorentino Department of Genetics, Duke University Medical Center, Durham, NC 27710. Search for more papers by this author J. Heitman J. Heitman Department of Genetics, Duke University Medical Center, Durham, NC 27710. Search for more papers by this author Author Information M.E. Cardenas1, C. Hemenway1, R.S. Muir1, R. Ye1, D. Fiorentino1 and J. Heitman1 1Department of Genetics, Duke University Medical Center, Durham, NC 27710. The EMBO Journal (1994)13:5944-5957https://doi.org/10.1002/j.1460-2075.1994.tb06940.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info The peptidyl-prolyl isomerases FKBP12 and cyclophilin A (immunophilins) form complexes with the immunosuppressants FK506 and cyclosporin A that inhibit the phosphatase calcineurin. With the yeast two hybrid system, we detect complexes between FKBP12 and the calcineurin A catalytic subunit in both the presence and absence of FK506. Mutations in FKBP12 surface residues or the absence of the calcineurin B regulatory subunit perturb the FK506-dependent, but not the ligand-independent, FKBP12-calcineurin complex. By affinity chromatography, both FKBP12 and cyclophilin A bind calcineurin A in the absence of ligand, and FK506 and cyclosporin A respectively potentiate these interactions. Both in vivo and in vitro, the peptidyl-prolyl isomerase active sites are dispensable for ligand-independent immunophilin-calcineurin complexes. Lastly, by genetic analyses we demonstrate that FKBP12 modulates calcineurin functions in vivo. These findings reveal that immunophilins interact with calcineurin in the absence of exogenous ligands and suggest that immunosuppressants may take advantage of the inherent ability of immunophilins to interact with calcineurin. Previous ArticleNext Article Volume 13Issue 241 December 1994In this issue RelatedDetailsLoading ..." @default.
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- W62803312 title "Immunophilins interact with calcineurin in the absence of exogenous immunosuppressive ligands." @default.
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- W62803312 doi "https://doi.org/10.1002/j.1460-2075.1994.tb06940.x" @default.
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