Cited by 637Cell death mechanisms and regulationMitochondrial Function and PathologyAutophagy in Disease and Therapy

The DOI matches its Crossref record; 263 of the 263 references it cites were found in a registry or an index.

The Mitochondrial Pathways of Apoptosis

Open access
Estaquier, Jérome, Vallette, François, Vayssiere, Jean-Luc, Mignotte, Bernard·2012·Advances in experimental medicine and biology

Abstract

Apoptosis is a process of programmed cell death that serves as a major mechanism for the precise regulation of cell numbers, and as a defense mechanism to remove unwanted and potentially dangerous cells. Studies in nematode, Drosophila and mammals have shown that, although regulation of the cell death machinery is somehow different from one species to another, it is controlled by homologous proteins and involves mitochondria. In mammals, activation of caspases (cysteine proteases that are the main executioners of apoptosis) is under the tight control of the Bcl-2 family proteins, named in reference to the first discovered mammalian cell death regulator. These proteins mainly act by regulating the release of caspases activators from mitochondria. Although for a long time the absence of mitochondrial changes was considered as a hallmark of apoptosis, mitochondria appear today as the central executioner of apoptosis. In this chapter, we present the current view on the mitochondrial pathway of apoptosis with a particular attention to new aspects of the regulation of the Bcl-2 proteins family control of mitochondrial membrane permeabilization: the mechanisms implicated in their mitochondrial targeting and activation during apoptosis, the function(s) of the oncosuppressive protein p53 at the mitochondria and the role of the processes of mitochondrial fusion and fission.

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Crossref · 10.1007/978-94-007-2869-1_7

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Research works printed but not linked: 3

  1. Chen ZX, Pervaiz S (2009a) BCL-2: pro-or anti-oxidant? Front Biosci (Elite Ed) 1:263–268
  2. Park HH, Lo YC, Lin SC, Wang L, Yang JK, Wu H (2007) The death domain superfamily in intracellular signaling of apoptosis and inflammation. Annu Rev Immunol 25:561–586 · DOI
  3. Sandu C, Ryoo HD, Steller H (2010) J Cell Biol 190:1039–1052 · DOI

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Metadata

Authors
Estaquier, J., Vallette, F., Vayssiere, J.-L., & Mignotte, B.
Affiliations
  • Centre National de la Recherche Scientifique (FR)
  • École Pratique des Hautes Études (FR)
Corresponding author
Mignotte, Bernard
Venue
Advances in experimental medicine and biology
Published
2011-12-22
Volume
942
Pages
157-183
ISSN
0065-2598 (ISSN-L)
OpenAlex
W116732461
Cited by
637
References
263
Citations by year
2026: 15 · 2025: 42 · 2024: 41 · 2023: 75 · 2022: 75 · 2021: 57 · 2020: 52 · 2019: 37 · 2018: 42 · 2017: 23 · 2016: 36 · 2015: 49 · 2014: 35 · 2013: 42 · 2012: 15
FWCI
38.19
Type
book chapter
Language
en
Open access
Locations
  • Advances in experimental medicine and biology (publishedVersion)
  • PubMed (publishedVersion)
  • HAL (submittedVersion, other-oa)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Keywords
mitochondrial apoptosis, Bcl-2 family proteins, caspase activation, mitochondrial membrane permeabilization, p53, mitochondrial fusion, mitochondrial fission, programmed cell death
MeSH terms
Animals, Enzyme Activation, Mitochondria, Apoptosis, Caspases

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