Decay of Endoplasmic Reticulum-Localized mRNAs During the Unfolded Protein Response

By J. Hollien, Jonathan S. Weissman. Science, 2006

1,209 citations recorded by the source corpus.

Subfields: Cell Biology, Epidemiology, Surgery

View Paper: https://www.semanticscholar.org/paper/43396b3968e58d3a1e85cf496367a09755abb246

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

1. C. Hetz
2. R. Kaufman
3. G. Hotamışlıgil
4. F. Papa
5. D. Ron
6. Peter Walter
7. I. Tabas
8. John Calvin Reed

In Epidemiology

1. C. Hetz
2. R. Kaufman
3. G. Hotamışlıgil
4. F. Papa
5. Peter Walter
6. D. Ron
7. John Calvin Reed
8. É. Chevet

In Surgery

1. R. Kaufman
2. C. Hetz
3. G. Hotamışlıgil
4. F. Papa
5. Peter Walter
6. D. Ron
7. I. Tabas
8. É. Chevet

Citations in the corpus

• Endoplasmic Reticulum Stress and the Inflammatory Basis of Metabolic Disease (2010, positive): “These mRNAs are degraded by IRE1, thereby preventing their translation, an additional measure to relieve ER stress (Hollien et al., 2009; Hollien and Weissman, 2006).”
• Endoplasmic reticulum stress signalling and the pathogenesis of non-alcoholic fatty liver disease. (2018, background): “specificity to degrade many other ER-bound mRNAs, including itself, at both stem-loop and non-stemloop sites, through regulated IRE1α-dependent decay (RIDD)(19-21).”
• Human Coronavirus: Host-Pathogen Interaction. (2019, background): “F or p er so na l u se o nl y. Nucleus Unfolded proteins PP PERK PP IRE1 ATF6 eIF2α eIF2αP Global protein translation CHOP GADD34 PP1 ATF4 CRE dsRNA PKR PKR PKR PP nsp15 (SARS, 229E, MHV) MERS 4a RIDD JNK XBP1U XBP1S XBP1U mRNA Splicing XBP1S mRNA SARS E UPRE/ERSE ER-associated mRNA Apoptosis S (MHV”
• Signal integration in the endoplasmic reticulum unfolded protein response (2007, background): “Recently, analysis of mRNAs expressed in ER-stressed Drosophila melanogaster cells uncovered evidence for widespread IRE1-dependent degradation of ER-associated mRNA”
• Regulated Ire1-dependent decay of messenger RNAs in mammalian cells (2009, background): “We have recently shown that Ire1 in Drosophila melanogaster cells independently mediates the cleavage and degradation of mRNAs encoding proteins that traverse the secretory pathway (Hollien and Weissman, 2006).”
• Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress (2011, background): “Under certain conditions, the IRE1 nuclease can also degrade and thus block the translation of a wide variety of mRNA species, although the possible physiologic and pathologic functions of this action are still being investigate”
• Protein quality control in the early secretory pathway (2008, background): “…tran- scription of genes enhancing protein folding (ER-resident chaperones and folding enzymes) and ERAD, (iii) decreased entry of proteins into the ER (Kang et al, 2006; Orsi et al, 2006) and (iv) selective degradation of certain mRNAs encoding secretory proteins (Hollien and Weissman, 2006).”
• Endoplasmic Reticulum Stress in Liver Disease (2010, background): “The IRE1α RNase activity is also implicated in the degradation of several cellular mRNAs, a process named regulated IRE1-dependenet decay (RIDD) [51-52], including proinsulin mRNA and IRE1α mRNA itself [42, 131].”
• Endoplasmic reticulum stress in disease pathogenesis. (2008, background): “In Drosophila cells, IRE1 activation by the strong reducing agent dithiothreitol triggered the cleavage and ensuing decay of a large set of mRNAs (16).”
• The Unfolded Protein Response and Cell Fate Control. (2017, positive): “In contrast, the activity of RIDD under increased IRE1a oligomerization appears sustained over time, 6 Molecular Cell 69, January 18, 2018 contributing to cell death (Ghosh et al., 2014).”