Caspase-mediated cleavage of Beclin-1 inactivates Beclin-1-induced autophagy and enhances apoptosis by promoting the release of proapoptotic factors from mitochondria

@inproceedings{Wirawan2010CaspasemediatedCO,
  title={Caspase-mediated cleavage of Beclin-1 inactivates Beclin-1-induced autophagy and enhances apoptosis by promoting the release of proapoptotic factors from mitochondria},
  author={Ellen Wirawan and Lieselotte Vande Walle and Kristof Kersse and Sigrid Cornelis and Sofie Claerhout and Isabel Vanoverberghe and Ria Roelandt and Riet De Rycke and Jelle Verspurten and Wim Declercq and Patrizia Agostinis and Tom Vanden Berghe and Saskia Lippens and Peter Vandenabeele},
  booktitle={Cell Death and Disease},
  year={2010}
}
Autophagy and apoptosis are two important and interconnected stress-response mechanisms. However, the molecular interplay between these two pathways is not fully understood. To study the fate and function of autophagic proteins at the onset of apoptosis, we used a cellular model system in which autophagy precedes apoptosis. IL-3 depletion of Ba/F3 cells caused caspase (casp)-mediated cleavage of Beclin-1 and PI3KC3, two crucial components of the autophagy-inducing complex. We identified two… CONTINUE READING
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