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The unfolded protein response at the crossroads of cellular life and death during endoplasmic reticulum stress

(2012) BIOLOGY OF THE CELL. 104(5). p.259-270
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Ghent researchers on unfolded proteins in inflammatory disease (GROUP-ID)
Project
Ghent researchers on unfolded proteins in inflammatory disease (GROUP-ID)
Abstract
One of the early cellular responses to endoplasmic reticulum (ER) stress is the activation of the unfolded protein response (UPR). ER stress and the UPR are both implicated in numerous human diseases and pathologies. In spite of this, our knowledge of the molecular mechanisms that regulate cell fate following ER stress is limited. The UPR is initiated by three ER transmembrane receptors: PKR-like ER kinase (PERK), activating transcription factor (ATF) 6 and inositol-requiring enzyme 1 (IRE1). These proteins sense the accumulation of unfolded proteins and their activation triggers specific adaptive responses to resolve the stress. Intriguingly, the very same receptors can initiate signalling pathways that lead to apoptosis when the attempts to resolve the ER stress fail. In this review, we describe the known pro-apoptotic signalling pathways emanating from activated PERK, ATF6 and IRE1 and discuss how their signalling switches from an adaptive to a pro-apoptotic response.
Keywords
Apoptosis, Endoplasmic reticulum, Unfolded protein response, ACTIVATING TRANSCRIPTION FACTOR-6, ER STRESS, INDUCED APOPTOSIS, TRANSMEMBRANE PROTEIN, MAMMALIAN-CELLS, MESSENGER-RNAS, IRE1 KINASE, ATF6, IRE1-ALPHA, CASPASE-12

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Citation

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Chicago
Jäger, Richard, Mathieu Bertrand, Adrienne M Gorman, Peter Vandenabeele, and Afshin Samali. 2012. “The Unfolded Protein Response at the Crossroads of Cellular Life and Death During Endoplasmic Reticulum Stress.” Biology of the Cell 104 (5): 259–270.
APA
Jäger, R., Bertrand, M., Gorman, A. M., Vandenabeele, P., & Samali, A. (2012). The unfolded protein response at the crossroads of cellular life and death during endoplasmic reticulum stress. BIOLOGY OF THE CELL, 104(5), 259–270.
Vancouver
1.
Jäger R, Bertrand M, Gorman AM, Vandenabeele P, Samali A. The unfolded protein response at the crossroads of cellular life and death during endoplasmic reticulum stress. BIOLOGY OF THE CELL. 2012;104(5):259–70.
MLA
Jäger, Richard, Mathieu Bertrand, Adrienne M Gorman, et al. “The Unfolded Protein Response at the Crossroads of Cellular Life and Death During Endoplasmic Reticulum Stress.” BIOLOGY OF THE CELL 104.5 (2012): 259–270. Print.
@article{2914156,
  abstract     = {One of the early cellular responses to endoplasmic reticulum (ER) stress is the activation of the unfolded protein response (UPR). ER stress and the UPR are both implicated in numerous human diseases and pathologies. In spite of this, our knowledge of the molecular mechanisms that regulate cell fate following ER stress is limited. The UPR is initiated by three ER transmembrane receptors: PKR-like ER kinase (PERK), activating transcription factor (ATF) 6 and inositol-requiring enzyme 1 (IRE1). These proteins sense the accumulation of unfolded proteins and their activation triggers specific adaptive responses to resolve the stress. Intriguingly, the very same receptors can initiate signalling pathways that lead to apoptosis when the attempts to resolve the ER stress fail. In this review, we describe the known pro-apoptotic signalling pathways emanating from activated PERK, ATF6 and IRE1 and discuss how their signalling switches from an adaptive to a pro-apoptotic response.},
  author       = {J{\"a}ger, Richard and Bertrand, Mathieu and Gorman, Adrienne M and Vandenabeele, Peter and Samali, Afshin},
  issn         = {0248-4900},
  journal      = {BIOLOGY OF THE CELL},
  keyword      = {Apoptosis,Endoplasmic reticulum,Unfolded protein response,ACTIVATING TRANSCRIPTION FACTOR-6,ER STRESS,INDUCED APOPTOSIS,TRANSMEMBRANE PROTEIN,MAMMALIAN-CELLS,MESSENGER-RNAS,IRE1 KINASE,ATF6,IRE1-ALPHA,CASPASE-12},
  language     = {eng},
  number       = {5},
  pages        = {259--270},
  title        = {The unfolded protein response at the crossroads of cellular life and death during endoplasmic reticulum stress},
  url          = {http://dx.doi.org/10.1111/boc.201100055},
  volume       = {104},
  year         = {2012},
}

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