The CD95 Type I/Type II model

Barnhart, Bryan C.; Alappat, Elizabeth C.; Peter, Marcus E.

doi:10.1016/s1044-5323(03)00031-9

Cited by 419Cell death mechanisms and regulationCancer-related Molecular PathwaysDeath, Funerary Practices, and Mourning

The CD95 Type I/Type II model

Barnhart, Bryan C., Alappat, Elizabeth C., Peter, Marcus E.·2003·Seminars in Immunology

DOI 10.1016/s1044-5323(03)00031-9

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Abstract

CD95 (APO-1/Fas) has become the prototype of a death domain containing receptor and is the best studied member of the death receptors that activate the extrinsic apoptosis pathway. This pathway is initiated by recruitment and activation of caspase-8, an initiator caspase, in the death-inducing signaling complex (DISC) followed by direct cleavage of downstream effector caspases. In contrast, the intrinsic apoptosis pathway starts from within the cell either by direct activation of caspases or through intracellular changes such as DNA damage resulting in the release of a number of pro-apoptotic factors from the intermembrane space of mitochondria. The release of these factors results in the activation of another initiator caspase, caspase-9, and ultimately in the activation of effector caspases in a protein complex called the apoptosome. In recent years, it has become apparent that there is cross talk between the extrinsic and intrinsic pathway. In the death receptor pathway of apoptosis induction, the best characterized connection between the two pathways is the Bcl-2 family member Bid which translocates to mitochondria after cleavage by caspase-8 causing pro-apoptotic changes. Cells that die through CD95 without help from mitochondria are called Type I cells, whereas cells in which CD95-mediated death relies mostly on the intrinsic pathway are called Type II. This review focuses on recent developments in the delineation of the biochemistry and the physiological function of the two CD95 pathways.

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In type I cells (e.g., thymocytes and mature lymphocytes), CASP8-dependent proteolytic maturation of executioner CASP3 and CASP7 suffices to drive RCD, which cannot be inhibited by transgene-driven overexpression of anti-apoptotic BCL2 proteins, co-deletion of Bax and Bak1, or loss of BID.
“In so-called “type I cells” (e.g., thymocytes and mature lymphocytes) the CASP8-dependent proteolytic maturation of executioner CASP3 and CASP7 suffices to drive RCD, which cannot be inhibited by the transgene-driven overexpression of anti-apoptotic BCL2 proteins, the co-deletion of Bax and Bak1, or the loss of BID [308, 309].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [308]

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Authors: Barnhart, B. C., Alappat, E. C., & Peter, M. E.
Affiliations: University of Chicago (US)
Corresponding author: Peter, Marcus E.
ORCID: Barnhart, Bryan C.
Peter, Marcus E.
Venue: Seminars in Immunology
Publisher: Elsevier BV
Published: 2003-06
Volume: 15
Issue: 3
Pages: 185-193
ISSN: 1044-5323 (ISSN-L)
DOI: 10.1016/s1044-5323(03)00031-9
OpenAlex: W2098641105
Cited by: 419
References: 79
Citations by year: 2026: 3 · 2025: 5 · 2024: 4 · 2023: 9 · 2022: 9 · 2021: 9 · 2020: 8 · 2019: 9 · 2018: 9 · 2017: 8 · 2016: 11 · 2015: 13 · 2014: 15 · 2013: 28 · 2012: 25
FWCI: 10.34
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Seminars in Immunology (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Institute of General Medical Sciences (GM61712, R01GM061712)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Social Sciences › Anthropology › Death, Funerary Practices, and Mourning
Keywords: Fas, death receptors, extrinsic apoptotic pathway, mitochondrial apoptosis, caspase-8, caspase-9, apoptosome, death-inducing signaling complex, Bcl-2 family proteins, Bid
MeSH terms: Animals, Humans, Membrane Glycoproteins, Mitochondria, Signal Transduction, Models, Immunological, fas Receptor, Fas Ligand Protein

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The CD95 Type I/Type II model

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