有哪些信誉好的足球投注网站cyclosporine a-sensitive, cyclophilin b-dependent endoplasmic reticulum-associated degradation环孢霉素敏感,还有b-dependent内质的reticulum-associated退化.pdfVIP
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cyclosporine a-sensitive, cyclophilin b-dependent endoplasmic reticulum-associated degradation环孢霉素敏感,还有b-dependent内质的reticulum-associated退化
Cyclosporine A-Sensitive, Cyclophilin B-Dependent Endoplasmic Reticulum-Associated Degradation 1. ` 1. 1. 1,2. 1,2 Riccardo Bernasconi , Tatiana Solda , Carmela Galli , Thomas Pertel , Jeremy Luban , Maurizio Molinari1,3* 1 Institute for Research in Biomedicine, Bellinzona, Switzerland, 2 Department of Microbiology and Molecular Medicine, University of Geneva, Geneva, Switzerland, 3 Ecole ´ ´ Polytechnique Federale de Lausanne, School of Life Sciences, Lausanne, Switzerland Abstract Peptidyl-prolyl cis/trans isomerases (PPIs) catalyze cis/trans isomerization of peptide bonds preceding proline residues. The involvement of PPI family members in protein refolding has been established in test tube experiments. Surprisingly, however, no data is available on the involvement of endoplasmic reticulum (ER)-resident members of the PPI family in protein folding, quality control or disposal in the living cell. Here we report that the immunosuppressive drug cyclosporine A (CsA) selectively inhibits the degradation of a subset of misfolded proteins generated in the ER. We identify cyclophilin B (CyPB) as the ER-resident target of CsA that catalytically enhances disposal from the ER of ERAD-LS substrates containing cis proline residues. Our manuscript presents the first evidence for enzymatic involvement of a PPI in protein quality control in the ER of living cells. ` Citation: Bernasconi R, Solda T, Galli C, Pertel T, Luban J, et al. (2010) Cyclosporine A-Sensitive, Cyclophilin B-Dependent Endoplasmic Reticulum-Associated Degradation. PLoS ONE 5(9): e13008. doi:10.1371/journal.pone.0013008 Editor: Suzannah Rutherfo
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