IRE1 Signaling Affects Cell Fate During the Unfolded Protein Response
By Jonathan H. Lin, Han Li, D. Yasumura, H. Cohen, Chao Zhang, B. Panning, Kevan M. Shokat, M. Lavail, Peter Walter. Science, 2007
1,392 citations recorded by the source corpus.
Subfields: Cell Biology, Epidemiology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/e89bfd4b4424c98d47008d3e71f04131f844c61d
How researchers see this paper
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In Cell Biology
- C. Hetz
- G. Hotamışlıgil
- R. Kaufman
- F. Papa
- Laurie H. Glimcher
- J. Cubillos-Ruiz
- Sarah Bettigole
- Peter Walter
In Epidemiology
- C. Hetz
- G. Hotamışlıgil
- R. Kaufman
- F. Papa
- Laurie H. Glimcher
- J. Cubillos-Ruiz
- Herbert Tilg
- Peter Walter
In Molecular Biology
- C. Hetz
- G. Hotamışlıgil
- R. Kaufman
- F. Papa
- Laurie H. Glimcher
- Ann-Hwee Lee
- J. Cubillos-Ruiz
- Luke A. Gilbert
Citations in the corpus
- Endoplasmic Reticulum Stress and the Inflammatory Basis of Metabolic Disease (2010, positive): “For example, attenuation of IRE1 and ATF6 activities by persistent ER stress and prolonged signaling through PERK can create an appropriate condition for apoptosis (Lin et al., 2007).”
- Regulated Ire1-dependent decay of messenger RNAs in mammalian cells (2009, background): “Bypassing the kinase activity of Ire1 Recently, it has been shown that for yeast and human Ire1, the cytoplasmic kinase activity can be bypassed using a small molecule that binds to the enlarged ATP pocket of an engineered Ire1 variant (Papa et al., 2003; Lin et al., 2007).”
- Tumorigenic and Immunosuppressive Effects of Endoplasmic Reticulum Stress in Cancer (2017, positive): “XBP1 induction favors cell survival, as enforced overexpression rescues cell viability in vitro and in a transgenic rat model of retinitis pigmentosa (Lin et al., 2007).”
- A multiplexed single-cell CRISPR screening platform enables systematic dissection of the unfolded protein response (2016, result): “These results were in contrast to transient XBP1 splicing caused by chemical stress, which diminished on the scale of hours, consistent with previous reports (Figure S4A) (Lin et al., 2007).”
- XBP1 links ER stress to intestinal inflammation and confers genetic risk for human inflammatory bowel disease (2008, positive): “XBP1 Deficiency Results in Enhanced Responses of IECs to Typical Mucosal Inflammatory Signals XBP1 mRNA splicing is a marker of IRE1 activation and ER stress (Calfon et al., 2002; Lin et al., 2007).”
- Endoplasmic reticulum stress: molecular mechanism and therapeutic targets (2023, background): “8,13 The downstream effects of ER stress can be involved in ERAD, protein synthesis, autophagy, oxidative stress, mitochondrial dysfunction, and metabolism.”
- The unfolded protein response protects human tumor cells during hypoxia through regulation of the autophagy genes MAP1LC3B and ATG5. (2010, background): “Similarly, IRE-1 is also activated during hypoxia (22) and loss of XBP1 reduces hypoxia tolerance and tumor growth (22, 23).”
- The Unfolded Protein Response and Cell Fate Control. (2017, positive): “Under conditions of mild ER stress, activation of XBP1 mRNA splicing is transient, leading to its attenuation after prolonged stimulation, which may sensitize cells to undergo apoptosis (Lin et al., 2007).”
- Endoplasmic Reticulum Stress in Liver Disease (2010, background): “However, in ER-stressed cells, XBP1 splicing and protein expression decline with time [81].”
- Cellular Stress Responses: Cell Survival and Cell Death (2010, background): “However, recently it has been shown that attenuation of IRE1 can switch the adaptive UPR to apoptosis and that persistent activation of IRE1 increases cell viability upon ER stress, suggesting that the duration of IRE1 signaling may act as a switch [219].”