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Calpain-mediated cleavage of Atg5 switches autophagy to apoptosis

Yousefi, Shida, Perozzo, Remo, Schmid, Inès, Ziemiecki, Andrew, Schaffner, Thomas, Scapozza, Leonardo, Brunner, Thomas, Simon, Hans-Uwe·2006·Nature Cell Biology

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  2. Gozuacik, D. & Kimchi, A. Autophagy as a cell death and tumor suppressor mechanism. Oncogene 23, 2891–2906 (2004). · DOI
  3. Blommaart, E. F., Luiken, J. J. & Meijer, A. J. Autophagic proteolysis: control and specificity. Histochem. J. 29, 365–385 (1997). · DOI
  4. Yu, L. et al. Regulation of an ATG7–beclin 1 program of autophagic cell death by caspase-8. Science 304, 1500–1502 (2004). · DOI
  5. Shimizu, S. et al. Role of Bcl-2 family proteins in a non-apoptotic programmed cell death dependent on autophagy genes. Nature Cell Biol. 6, 1221–1228 (2004). · DOI · Paper page
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  7. Goldstein, J. C., Waterhouse, N. J., Juin, P., Evan, G. I. & Green, D. R. The coordinate release of cytochrome c during apoptosis is rapid, complete and kinetically invariant. Nature Cell Biol. 2, 156–162 (2000). · DOI
  8. Simon, H.-U. Neutrophil apoptosis pathways and their modifications in inflammation. Immunol. Rev. 193, 101–110 (2003). · DOI
  9. Gao, G. & Dou, Q. P. N-terminal cleavage of Bax by calpain generates a potent proapoptotic 18-kDa fragment that promotes Bcl-2-independent cytochrome c release and apoptotic cell death. J. Cell Biochem. 80, 53–72 (2000). · DOI
  10. Altznauer, F., Conus, S., Cavalli, A., Folkers, G. & Simon, H.-U. Calpain-1 regulates Bax and subsequent Smac-dependent caspase-3 activation in neutrophil apoptosis. J. Biol. Chem. 279, 5947–5957 (2004). · DOI
  11. Arthur, J. S., Elce, J. S., Hegadorn, C., Williams, K. & Greer, P. A. Disruption of the murine calpain small subunit gene, Capn4: calpain is essential for embryonic development but not for cell growth and division. Mol. Cell. Biol. 20, 4474–4481 (2000). · DOI
  12. Martin, S. J. et al. Early redistribution of plasma membrane phosphatidylserine is a general feature of apoptosis regardless of the initiating stimulus: Inhibition by overexpression of Bcl-2 and Abl. J. Exp. Med. 182, 1545–1556 (1995). · DOI · Paper page
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  15. Mihara, M. et al. p53 has a direct apoptogenic role at the mitochondria. Mol. Cell 11, 577–590 (2003). · DOI
  16. Leu, J. I., Dumont, P., Hafey, M., Murphy, M. E. & George, D. L. Mitochondrial p53 activates Bak and causes disruption of a Bak-Mcl1 complex. Nature Cell Biol. 6, 443–450 (2004). · DOI
  17. Li, H. et al. Cytochrome c release and apoptosis induced by mitochondrial targeting of nuclear orphan receptor TR3. Science 289, 1159–1164 (2000). · DOI
  18. Karuman, P. et al. The Peutz-Jegher gene product LKB1 is a mediator of p53-dependent cell death. Mol. Cell 7, 1307–1319 (2001). · DOI
  19. Chua, B. T. et al. Mitochondrial translocation of cofilin is an early step in apoptosis induction. Nature Cell Biol. 5, 1083–1089 (2003). · DOI
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  21. Simon, H.-U. et al. Eosinophils maintain their capacity to signal and release eosinophil cationic protein upon repetitive stimulation with the same agonist. J. Immunol. 165, 4069–4075 (2000). · DOI
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  29. Bovia, F. et al. Efficient transduction of primary human B lymphocytes and nondividing myeloma B cells with HIV-1-derived lentiviral vectors. Blood 101, 1727–1733 (2003). · DOI
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Metadata

Authors
Yousefi, S., Perozzo, R., Schmid, I., Ziemiecki, A., Schaffner, T., Scapozza, L., Brunner, T., & Simon, H.-U.
Venue
Nature Cell Biology
Published
2006-09-24
Volume
8
Issue
10
Pages
1124-1132
ISSN
  • 1465-7392
  • 1476-4679
Cited by
1,158
References
3
Language
en

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