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Extra info for Dislocation and Degradation of Proteins from the Endoplasmic Reticulum (Current Topics in Microbiology and Immunology)

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References Ahner A, Brodsky JL (2004) Checkpoints in ER-associated degradation: excuse me, which way to the proteasome? Trends Cell Biol. 14:474–478 Akiyama Y, Ito K (2003) Reconstitution of membrane proteolysis by FtsH. J Biol Chem 278:18146–18153 Aridor M, Hannan LA (2000) Traffic jam: a compendium of human diseases that affect intracellular transport processes. Traffic 1:836–851 Aridor M, Hannan LA (2002) Traffic jams II: an update of diseases of intracellular transport. Traffic 3:781–790 Recognition and Delivery of ERAD Substrates 33 Arvan P, Zhao X, Ramos-Castaneda J, Chang A (2002) Secretory pathway quality control operating in Golgi, plasmalemmal, and endosomal systems.

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.

However, it is clear that the formation of both aggresomes and ER aggregates rise when the proteasome is compromised (Kopito 2000), suggesting that a change in the concentration of misfolded proteins contributes to aggregate formation. Thus, it has been noted that therapies that decrease proteasome function in vivo might have severe, secondary consequences (Ma et al. 2002). 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.

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