Cited by 641Cell death mechanisms and regulationCancer-related Molecular PathwaysHeat shock proteins research

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Mechanisms of p53-dependent apoptosis

Schuler, M., Green, D. R.·2001·Biochemical Society Transactions

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Abstract

Cellular stresses, such as growth factor deprivation, DNA damage or oncogene expression, lead to stabilization and activation of the p53 tumour suppressor protein. Depending on the cellular context, this results in one of two different outcomes: cell cycle arrest or apoptotic cell death. Cell death induced through the p53 pathway is executed by the caspase proteinases, which, by cleaving their substrates, lead to the characteristic apoptotic phenotype. Caspase activation by p53 occurs through the release of apoptogenic factors from the mitochondria, including cytochrome c and Smac/DIABLO. Released cytochrome c allows the formation of a high-molecular weight complex, the apoptosome, which consists of the adapter protein Apaf-1 and caspase 9, which is activated following recruitment into the apoptosome. Active caspase 9 then cleaves and activates the effector caspases, such as caspases-3 and -7, which execute the death program. Released Smac/DIABLO facilitates caspase activation through repression of the IAP caspase inhibitor proteins. The release of mitochondrial apoptogenic factors is regulated by the pro- and anti-apoptotic Bcl-2 family proteins, which either induce or prevent the permeabilization of the outer mitochondrial membrane. The mechanism by which p53 signals to the Bcl-2 family proteins is unclear. It was shown that some of the pro-apoptotic family members, such as Bax, Noxa or PUMA, are transcriptional targets of p53. In addition, transcription-independent, pro-apoptotic activities of p53 have been described. The elucidation of the p53-dependent pathway, resulting in mitochondrial outer membrane permeabilization through the pro-apoptotic Bcl-2 family proteins, is a key to unveiling the mechanism of stress-induced apoptosis.

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Authors: Schuler, M., & Green, D. R.
Affiliations: Department of Medicine III, Johannes Gutenberg University, 55101 Mainz, Germany
La Jolla Institute for Immunology (US)
ORCID: Green, D. R.
Venue: Biochemical Society Transactions
Publisher: Portland Press Ltd.
Published: 2001-11-01
Volume: 29
Issue: 6
Pages: 684-688
ISSN: 0300-5127 (ISSN-L)
1470-8752
DOI: 10.1042/bst0290684
OpenAlex: W2091766574
Cited by: 641
References: 0
Citations by year: 2026: 9 · 2025: 20 · 2024: 15 · 2023: 17 · 2022: 18 · 2021: 13 · 2020: 29 · 2019: 25 · 2018: 22 · 2017: 21 · 2016: 23 · 2015: 22 · 2014: 25 · 2013: 26 · 2012: 38
FWCI: 11.33
Type: journal article
Language: en
Open access: closed
Locations: Biochemical Society Transactions (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Keywords: p53, apoptosis, caspase activation, apoptosome, cytochrome c, Smac/DIABLO, IAP inhibitors, Bcl-2 family proteins, mitochondrial outer membrane permeabilization, Bax, Noxa, PUMA, cell cycle arrest, DNA damage, growth factor deprivation, oncogene expression
MeSH terms: Animals, Enzyme Activation, Humans, Mitochondria, Models, Biological, Transcription, Genetic, Tumor Suppressor Protein p53, Apoptosis, Caspases

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