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

Hadi Khalil, Mathieu Bertrand UGent, Peter Vandenabeele UGent and Christian Widmann (2014) TRENDS IN CELL BIOLOGY. 24(2). p.83-89
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).
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (review)
publication status
published
subject
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
journal title
TRENDS IN CELL BIOLOGY
Trends Cell Biol.
volume
24
issue
2
pages
83 - 89
Web of Science type
Review
Web of Science id
000332498100001
JCR category
CELL BIOLOGY
JCR impact factor
12.007 (2014)
JCR rank
14/184 (2014)
JCR quartile
1 (2014)
ISSN
0962-8924
DOI
10.1016/j.tcb.2013.08.002
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
4375625
handle
http://hdl.handle.net/1854/LU-4375625
date created
2014-04-30 12:43:55
date last changed
2016-12-19 15:38:32
@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},
}

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.