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Extra info for Dislocation and Degradation of Proteins from the Endoplasmic Reticulum (Current Topics in Microbiology and Immunology)
Example text
51 Abstract CPY* is a mutated and malfolded secretory enzyme (carboxypeptidase yscY, Gly255Arg), which is imported into the endoplasmic reticulum but never reaches the vacuole, the destination of its wild type counterpart. Its creation, through mutation, had a major impact on the elucidation of the mechanisms of quality control and associated protein degradation of the endoplasmic reticulum, the eukaryotic organelle, where secretory proteins start the passage to their site of action.
Nature 404:770–774 Shamu CE, Flierman D, Ploegh HL, Rapoport TA, Chau V (2001) Polyubiquitinylation is required for US11-dependent movement of MHC class I heavy chain from endoplasmic reticulum into cytosol. Mol Biol Cell 12:2546–2555 Shen Y, Meunier L, Hendershot LM (2002) Identification and characterization of a novel endoplasmic reticulum (ER) DnaJ homologue, which stimulates ATPase activity of BiP in vitro and is induced by ER stress. J Biol Chem 277:15947–15956 Sifers RN (2003) Cell biology.
Wolf · A. Schäfer the ER [13, 73]. In contrast to CPY*, degradation of nonglycosylated ER substrates was not affected by the absence of both Ca2+ pumps; Ca2+ homeostasis in the ER must be linked to the quality control mechanism of N-glycosylated proteins [73]. α1,2-Mannosidase I is a Ca2+ -dependent enzyme. Indeed, analysis of N-linked oligosaccharides in ∆pmr1∆cod1 double mutants uncovered a large portion of protein-linked sugar being of the untrimmed Man9 GlcNAc2 type [73]. This indicates that one function of ER-calcium in the degradation of CPY* rests in its ability to render α1,2-mannosidase I active and thus allow proper ER quality control of N-glycosylated proteins.
