Cited by 4,445Cell death mechanisms and regulationMitochondrial Function and PathologyAutophagy in Disease and Therapy

Cleavage of BID by Caspase 8 Mediates the Mitochondrial Damage in the Fas Pathway of Apoptosis

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Li, Honglin, Zhu, Hong, Xu, Chi-jie, Yuan, Junying·1998·Cell

Abstract

We report here that BID, a BH3 domain-containing proapoptotic Bcl2 family member, is a specific proximal substrate of Casp8 in the Fas apoptotic signaling pathway. While full-length BID is localized in cytosol, truncated BID (tBID) translocates to mitochondria and thus transduces apoptotic signals from cytoplasmic membrane to mitochondria. tBID induces first the clustering of mitochondria around the nuclei and release of cytochrome c independent of caspase activity, and then the loss of mitochondrial membrane potential, cell shrinkage, and nuclear condensation in a caspase-dependent fashion. Coexpression of BclxL inhibits all the apoptotic changes induced by tBID. Our results indicate that BID is a mediator of mitochondrial damage induced by Casp8.

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Crossref · 10.1016/s0092-8674(00)81590-1

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Authors
Li, H., Zhu, H., Xu, C.-J., & Yuan, J.
Affiliations
Harvard University (US)
Corresponding author
Yuan, Junying
Venue
Cell
Publisher
Elsevier BV
Published
1998-08
Volume
94
Issue
4
Pages
491-501
ISSN
0092-8674 (ISSN-L)
OpenAlex
W2062853648
Cited by
4,445
References
0
Citations by year
2026: 42 · 2025: 64 · 2024: 55 · 2023: 70 · 2022: 56 · 2021: 116 · 2020: 69 · 2019: 88 · 2018: 91 · 2017: 111 · 2016: 123 · 2015: 115 · 2014: 137 · 2013: 159 · 2012: 183
FWCI
80.91
Type
journal article
Language
en
Open access
Locations
  • Cell (publishedVersion)
  • PubMed (publishedVersion)
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
  • Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
Keywords
Bid, caspase-8, mitochondrial damage, truncated Bid, mitochondrial translocation, cytochrome c release, mitochondrial membrane potential, Bcl-xL, Bcl-2 family proteins, apoptosis, BH3 domain
MeSH terms
Animals, Carrier Proteins, Cell Nucleus, Cysteine Endopeptidases, Cytochrome c Group, Humans, Mitochondria, Peptide Fragments, Substrate Specificity, Tumor Necrosis Factor-alpha, Signal Transduction, Apoptosis, fas Receptor, Proto-Oncogene Proteins c-bcl-2, Caspases, Cell Size, bcl-X Protein, BH3 Interacting Domain Death Agonist Protein, Mice, Caspase 8, Caspase 9

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