Abstract：
:The unfolded protein response (UPR) regulates gene expression in response to stress in the endoplasmic reticulum (ER). We determined the transcriptional scope of the UPR using DNA microarrays. Rather than regulating only ER-resident chaperones and phospholipid biosynthesis, as anticipated from earlier work, the UPR affects multiple ER and secretory pathway functions. Studies of UPR targets engaged in ER-associated protein degradation (ERAD) reveal an intimate coordination between these responses: efficient ERAD requires an intact UPR, and UPR induction increases ERAD capacity. Conversely, loss of ERAD leads to constitutive UPR induction. Finally, simultaneous loss of ERAD and the UPR greatly decreases cell viability. Thus, the UPR and ERAD are dynamic responses required for the coordinated disposal of misfolded proteins even in the absence of acute stress.
journal_name
Celljournal_title
Cellauthors
Travers KJ,Patil CK,Wodicka L,Lockhart DJ,Weissman JS,Walter Pdoi
10.1016/s0092-8674(00)80835-1subject
Has Abstractpub_date
2000-04-28 00:00:00pages
249-58issue
3eissn
0092-8674issn
1097-4172pii
S0092-8674(00)80835-1journal_volume
101pub_type
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