By E.J.H.J. Wiertz (Editor), M. Kikkert (Editor)
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Additional info for Dislocation and Degradation of Proteins from the Endoplasmic Reticulum (Current Topics in Microbiology and Immunology)
The establishment of yeast in the elucidation of the physiological function of vacuolar [77, 70, 78] and ubiquitin-proteasome linked proteolysis [32, 72] and the ﬁnding of CPY* as a rapidly degraded, malfolded secretory protein [20, 65, 61] were crucially important for the dissection of ER quality control and the associated cytosolic degradation pathway (ERQD). CPY* and the Power of Yeast Genetics 43 2 Endoplasmic Reticulum to Cytosol Retrotranslocation: A New Cellular Mechanism The isolation of yeast mutants defective in the degradation of CPY* started to give crucial insights into the quality control and degradation pathway .
44 4 Soluble Proteins Require Endoplasmic Reticulum-Lumenal Chaperones for Degradation . . . . . . . . . . . . . . . . 46 5 Sec61p, Part of the Retrotranslocation Channel? . . . . . . . . . 46 6 Endoplasmic Reticulum-Associated Protein Degradation: Ubiquitin, the Proteasome and Other Helpers . . . . . . . . . . 47 7 Modular CPY*-Based Membrane Substrates Broaden the Picture . . . 48 8 Yeast Genomics Discovers New Players . . . . . . . . . . .
Can a Protein’s Conformation or ERAD Be Modulated to Prevent Disease? Many studies indicate that “chemical chaperones” facilitate the maturation and folding of mutated or unstable proteins (Tamarappoo and Verkman 1998; Song and Chuang 2001; Sawkar et al. 2002; Noorwez et al. 2003). Chemical chaperones are most commonly osmolytes that facilitate protein folding, either by ordering water and strengthening intramolecular bonds, or by helping solvate proteins in the process of folding. Other chemical chaperones are enzyme 32 A.