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2003). However, only select ERAD substrates have been shown to utilize this pathway, and it is possible that other, as yet unknown, factors facilitate ERAD substrate selection. For example, nonglycosylated proteins do not interact efficiently with calnexin, and yeast lack UGGT. In mammals, some glycoproteins waiting for protein partners in the ER are fairly stable (Vanhove et al. 2001 and references therein), suggesting that immature glycoproteins are not degraded rapidly via ERAD; thus, EDEM selection might be overridden.

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 . . . . . . . . . . . . . 50 References . . . . . . . . . . . . . . . . . . . . . . . . . 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.

43 3 Carbohydrate Trimming: A Tool of the Endoplasmic Reticulum Quality Control of Glycoproteins . . . . . . . . . . . . . . . 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 .

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