| Cell, Vol. 101, 249--258, April 28, 2000, Copyright 2000 by Cell Press (2000) | |||||||||||||
Abstract | |||||||||||||
| roarrays. Rather than (Cox and Walter, 1996; Mori et al., 1996; Sidrauski et al., 1996; Sidrauski and Walter, 1997), and ultimately regulating only ER-resident chaperones and phospholipid biosynthesis, as anticipated from earlier work, transcriptional induction of UPR target genes. Regulation of gene expression by the UPR allows the cell to the UPR affects multiple ER and secretory pathway functions. Studies of UPR targets engaged in ER-asso- tolerate folding stress and presumably assists in correction of the insult that caused unfolded proteins to accu- ciated protein degradation (ERAD) reveal an intimate coordination between these responses: efficient ERAD mulate (Cox et al., 1993; Mori et al., 1993). While the mechanism by which the UPR signal is requires an intact UPR, and UPR induction increases ERAD capacity. Conversely, loss of ERAD leads to transmitted from the ER to the nucleus is well characterized, it is less clear how this response corrects misfold- constitutive UPR | |||||||||||||
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