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Signal integration in the endoplasmic reticulum unfolded protein response
Together, at least three mechanistically distinct arms of the UPR regulate the expression of numerous genes that function within the secretory pathway but also affect broad aspects of cell fate and the metabolism of proteins, amino acids and lipids.
The Unfolded Protein Response: From Stress Pathway to Homeostatic Regulation
The vast majority of proteins that a cell secretes or displays on its surface first enter the endoplasmic reticulum (ER), where they fold and assemble. Only properly assembled proteins advance from…
Functional and Genomic Analyses Reveal an Essential Coordination between the Unfolded Protein Response and ER-Associated Degradation
Molecular Biology of the Cell (Fifth Edition)
A Novel Mechanism for Regulating Activity of a Transcription Factor That Controls the Unfolded Protein Response
Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase
IRE1 Signaling Affects Cell Fate During the Unfolded Protein Response
There is a causal link between the duration of UPR branch signaling and life or death cell fate after ER stress, and key findings from studies in cell culture were recapitulated in photoreceptors expressing mutant rhodopsin in animal models of retinitis pigmentosa.
Regulated Ire1-dependent decay of messenger RNAs in mammalian cells
- J. Hollien, Jonathan H. Lin, Han Li, N. Stevens, P. Walter, J. Weissman
- Biology, Computer ScienceThe Journal of cell biology
- 10 August 2009
It is shown that mouse fibroblasts expressing wild-type Ire1 but not an Ire1 variant lacking nuclease activity also degrade mRNAs in response to ER stress, suggesting that cells use a multitiered mechanism by which different conditions in the ER lead to distinct outputs from Ire1.
An ER-Mitochondria Tethering Complex Revealed by a Synthetic Biology Screen
A large-scale genetic interaction map suggests that these ER-mitochondria connections are important for interorganellar phospholipid exchange, and shows that discrete sites of close apposition between ER and mitochondria facilitate interorganelle calcium and phospholIPid exchange.