The yeast apoptosis field emerged with the finding that key components of the apoptotic machinery are conserved in these simple eukaryotes. Thus it became possible to exploit these genetically tractable organisms to improve our understanding of the intricate mechanisms of cell death in higher eukaryotes and of severe human diseases associated with apoptosis dysfunctions. Early on, it was recognized that a mitochondria-mediated apoptotic pathway showing similarities to the mammalian intrinsic pathway was conserved in yeast. Recently, lysosomes have also emerged as central players in mammalian apoptosis. Following LMP (lysosomal membrane permeabilization), lysosomal proteases such as cathepsins B, D and L are released into the cytosol and can trigger a mitochondrial apoptotic cascade. CatD (cathepsin D) can also have anti-apoptotic effects in some cellular types and specific contexts. Nonetheless, the mechanisms underlying LMP and the specific role of cathepsins after their release into the cytosol remain poorly understood. We have recently shown that yeast vacuoles, membrane-bound acidic organelles, which share many similarities to plant vacuoles and mammalian lysosomes, are also involved in the regulation of apoptosis and that the vacuolar protease Pep4p, orthologue of the human CatD, is released from the vacuole into the cytosol in response to acetic acid. Here, we discuss how the conservation of cell-death regulation mechanisms in yeast by the lysosome-like organelle and mitochondria may provide new insights into the understanding of the complex interplay between the mitochondria and lysosome-mediated signalling routes during mammalian apoptosis.
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October 2011
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Conference Article|
September 21 2011
Vacuole–mitochondrial cross-talk during apoptosis in yeast: a model for understanding lysosome–mitochondria-mediated apoptosis in mammals
Maria João Sousa;
Maria João Sousa
*CBMA (Centre of Molecular and Environmental Biology)/Department of Biology, University of Minho, Campus de Gualtar, 4710-057 Braga, Portugal
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Flávìa Azevedo;
Flávìa Azevedo
*CBMA (Centre of Molecular and Environmental Biology)/Department of Biology, University of Minho, Campus de Gualtar, 4710-057 Braga, Portugal
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Ana Pedras;
Ana Pedras
*CBMA (Centre of Molecular and Environmental Biology)/Department of Biology, University of Minho, Campus de Gualtar, 4710-057 Braga, Portugal
†CITAB (Centro de Investigação e de Tecnologias Agro-Ambientais e Biológicas), Vila Real, Portugal
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Carolina Marques;
Carolina Marques
*CBMA (Centre of Molecular and Environmental Biology)/Department of Biology, University of Minho, Campus de Gualtar, 4710-057 Braga, Portugal
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Olga P. Coutinho;
Olga P. Coutinho
*CBMA (Centre of Molecular and Environmental Biology)/Department of Biology, University of Minho, Campus de Gualtar, 4710-057 Braga, Portugal
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Ana Preto;
Ana Preto
*CBMA (Centre of Molecular and Environmental Biology)/Department of Biology, University of Minho, Campus de Gualtar, 4710-057 Braga, Portugal
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Hernâni Gerós;
Hernâni Gerós
†CITAB (Centro de Investigação e de Tecnologias Agro-Ambientais e Biológicas), Vila Real, Portugal
‡Department of Biology, University of Minho, Campus de Gualtar, 4710-057 Braga, Portugal
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Susana R. Chaves;
Susana R. Chaves
*CBMA (Centre of Molecular and Environmental Biology)/Department of Biology, University of Minho, Campus de Gualtar, 4710-057 Braga, Portugal
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Manuela Côrte-Real
Manuela Côrte-Real
1
*CBMA (Centre of Molecular and Environmental Biology)/Department of Biology, University of Minho, Campus de Gualtar, 4710-057 Braga, Portugal
1To whom correspondence should be addressed (email mcortereal@bio.uminho.pt).
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Publisher: Portland Press Ltd
Received:
May 31 2011
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2011 Biochemical Society
2011
Biochem Soc Trans (2011) 39 (5): 1533–1537.
Article history
Received:
May 31 2011
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Citation
Maria João Sousa, Flávìa Azevedo, Ana Pedras, Carolina Marques, Olga P. Coutinho, Ana Preto, Hernâni Gerós, Susana R. Chaves, Manuela Côrte-Real; Vacuole–mitochondrial cross-talk during apoptosis in yeast: a model for understanding lysosome–mitochondria-mediated apoptosis in mammals. Biochem Soc Trans 1 October 2011; 39 (5): 1533–1537. doi: https://doi.org/10.1042/BST0391533
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