Bid, a Bcl2 Interacting Protein, Mediates Cytochrome c Release from Mitochondria in Response to Activation of Cell Surface Death Receptors

Luo, Xu; Budihardjo, Imawati; Zou, Hua; Slaughter, Clive; Wang, Xiaodong

doi:10.1016/s0092-8674(00)81589-5

Cited by 3,626Cell death mechanisms and regulationMitochondrial Function and PathologyDeath, Funerary Practices, and Mourning

Bid, a Bcl2 Interacting Protein, Mediates Cytochrome c Release from Mitochondria in Response to Activation of Cell Surface Death Receptors

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Luo, Xu, Budihardjo, Imawati, Zou, Hua, Slaughter, Clive, Wang, Xiaodong·1998·Cell

DOI 10.1016/s0092-8674(00)81589-5

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Abstract

We report here the purification of a cytosolic protein that induces cytochrome c release from mitochondria in response to caspase-8, the apical caspase activated by cell surface death receptors such as Fas and TNF. Peptide mass fingerprinting identified this protein as Bid, a BH3 domain-containing protein known to interact with both Bcl2 and Bax. Caspase-8 cleaves Bid, and the COOH-terminal part translocates to mitochondria where it triggers cytochrome c release. Immunodepletion of Bid from cell extracts eliminated the cytochrome c releasing activity. The cytochrome c releasing activity of Bid was antagonized by Bcl2. A mutation at the BH3 domain diminished its cytochrome c releasing activity. Bid, therefore, relays an apoptotic signal from the cell surface to mitochondria.

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In type II cells, extrinsic apoptosis requires proteolytic cleavage of BID by CASP8.
“extrinsic apoptosis requires the proteolytic cleavage of BID by CASP8 [70, 311, 312].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [70]

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Authors: Luo, X., Budihardjo, I., Zou, H., Slaughter, C., & Wang, X.
Affiliations: Howard Hughes Medical Institute (US)
Corresponding author: Wang, Xiaodong
ORCID: Luo, Xu
Zou, Hua
Wang, Xiaodong
Venue: Cell
Publisher: Elsevier BV
Published: 1998-08
Volume: 94
Issue: 4
Pages: 481-490
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/s0092-8674(00)81589-5
OpenAlex: W2012173926
Cited by: 3,626
References: 53
Citations by year: 2026: 25 · 2025: 40 · 2024: 39 · 2023: 52 · 2022: 46 · 2021: 74 · 2020: 40 · 2019: 46 · 2018: 52 · 2017: 50 · 2016: 100 · 2015: 91 · 2014: 99 · 2013: 114 · 2012: 136
FWCI: 75.59
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 5464 d)
Locations: Cell (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Institute of General Medical Sciences (R01GM057158, R01GM-57158)
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
Social Sciences › Anthropology › Death, Funerary Practices, and Mourning
Keywords: Bid, cytochrome c release, mitochondrial apoptosis, death receptors, Fas, TNF-α, caspase-8, BH3 domain, Bcl-2, Bax, apoptosis signaling, protein translocation
MeSH terms: Amino Acid Sequence, Animals, Carrier Proteins, Cysteine Endopeptidases, Cytochrome c Group, HeLa Cells, Humans, Mitochondria, Liver, Molecular Sequence Data, Receptors, Cell Surface, Apoptosis, Sequence Analysis, fas Receptor, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Proto-Oncogene Proteins c-bcl-2, Caspases, BH3 Interacting Domain Death Agonist Protein, Mice, Caspase 8, Caspase 9

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Bid, a Bcl2 Interacting Protein, Mediates Cytochrome c Release from Mitochondria in Response to Activation of Cell Surface Death Receptors

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