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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-17347

Galluzzi, L; Joza, N; Tasdemir, E; Maiuri, M C; Hengartner, M; Abrams, J M; Tavernarakis, N; Penninger, J; Madeo, F; Kroemer, G (2008). No death without life: vital functions of apoptotic effectors. Cell Death and Differentiation, 15(7):1113-1123.

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Abstract

As a result of the genetic experiments performed in Caenorhabditis elegans, it has been tacitly assumed that the core proteins of the 'apoptotic machinery' (CED-3, -4, -9 and EGL-1) would be solely involved in cell death regulation/execution and would not exert any functions outside of the cell death realm. However, multiple studies indicate that the mammalian orthologs of these C. elegans proteins (i.e. caspases, Apaf-1 and multidomain proteins of the Bcl-2 family) participate in cell death-unrelated processes. Similarly, loss-of-function mutations of ced-4 compromise the mitotic arrest of DNA-damaged germline cells from adult nematodes, even in a context in which the apoptotic machinery is inoperative (for instance due to mutations of egl-1 or ced-3). Moreover, EGL-1 is required for the activation of autophagy in starved nematodes. Finally, the depletion of caspase-independent death effectors, such as apoptosis-inducing factor (AIF) and endonuclease G, provokes cell death-independent consequences, both in mammals and in yeast (Saccharomyces cerevisiae). These results corroborate the conjecture that any kind of protein that has previously been specifically implicated in apoptosis might have a phylogenetically conserved apoptosis-unrelated function, most likely as part of an adaptive response to cellular stress.

Item Type:Journal Article, refereed, further contribution
Communities & Collections:07 Faculty of Science > Institute of Molecular Life Sciences
DDC:570 Life sciences; biology
Language:English
Date:July 2008
Deposited On:07 Mar 2009 17:19
Last Modified:27 Nov 2013 20:12
Publisher:Nature Publishing Group
ISSN:1350-9047
Publisher DOI:10.1038/cdd.2008.28
PubMed ID:18309324
Citations:Web of Science®. Times Cited: 92
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Scopus®. Citation Count: 104

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