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Caspase-3 and RasGAP: a stress-sensing survival/demise switch

(2014) TRENDS IN CELL BIOLOGY. 24(2). p.83-89
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Abstract
The final decision on cell fate, survival versus cell death, relies on complex and tightly regulated checkpoint mechanisms. The caspase-3 protease is a predominant player in the execution of apoptosis. However, recent progress has shown that this protease paradoxically can also protect cells from death. Here, we discuss the underappreciated, protective, and prosurvival role of caspase-3 and detail the evidence showing that caspase-3, through differential processing of p120 Ras GTPase-activating protein (Ras-GAP), can modulate a given set of proteins to generate, depending on the intensity of the input signals, opposite outcomes (survival vs death).
Keywords
CELL-DEATH, UNFOLDED PROTEIN RESPONSE, INDUCED APOPTOSIS, ER STRESS, BETA-CELL, ACTIVATION, DIFFERENTIATION, CLEAVAGE, NF-KAPPA-B, cellular stress, sensors, ENDOPLASMIC-RETICULUM STRESS, RasGAP, caspase-3, apoptosis

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Citation

Please use this url to cite or link to this publication:

Chicago
Khalil, Hadi, Mathieu Bertrand, Peter Vandenabeele, and Christian Widmann. 2014. “Caspase-3 and RasGAP: a Stress-sensing Survival/demise Switch.” Trends in Cell Biology 24 (2): 83–89.
APA
Khalil, Hadi, Bertrand, M., Vandenabeele, P., & Widmann, C. (2014). Caspase-3 and RasGAP: a stress-sensing survival/demise switch. TRENDS IN CELL BIOLOGY, 24(2), 83–89.
Vancouver
1.
Khalil H, Bertrand M, Vandenabeele P, Widmann C. Caspase-3 and RasGAP: a stress-sensing survival/demise switch. TRENDS IN CELL BIOLOGY. 2014;24(2):83–9.
MLA
Khalil, Hadi, Mathieu Bertrand, Peter Vandenabeele, et al. “Caspase-3 and RasGAP: a Stress-sensing Survival/demise Switch.” TRENDS IN CELL BIOLOGY 24.2 (2014): 83–89. Print.
@article{4375625,
  abstract     = {The final decision on cell fate, survival versus cell death, relies on complex and tightly regulated checkpoint mechanisms. The caspase-3 protease is a predominant player in the execution of apoptosis. However, recent progress has shown that this protease paradoxically can also protect cells from death. Here, we discuss the underappreciated, protective, and prosurvival role of caspase-3 and detail the evidence showing that caspase-3, through differential processing of p120 Ras GTPase-activating protein (Ras-GAP), can modulate a given set of proteins to generate, depending on the intensity of the input signals, opposite outcomes (survival vs death).},
  author       = {Khalil, Hadi and Bertrand, Mathieu and Vandenabeele, Peter and Widmann, Christian},
  issn         = {0962-8924},
  journal      = {TRENDS IN CELL BIOLOGY},
  keyword      = {CELL-DEATH,UNFOLDED PROTEIN RESPONSE,INDUCED APOPTOSIS,ER STRESS,BETA-CELL,ACTIVATION,DIFFERENTIATION,CLEAVAGE,NF-KAPPA-B,cellular stress,sensors,ENDOPLASMIC-RETICULUM STRESS,RasGAP,caspase-3,apoptosis},
  language     = {eng},
  number       = {2},
  pages        = {83--89},
  title        = {Caspase-3 and RasGAP: a stress-sensing survival/demise switch},
  url          = {http://dx.doi.org/10.1016/j.tcb.2013.08.002},
  volume       = {24},
  year         = {2014},
}

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