Identification of the protein-protein contact site and interaction mode of human VDAC1 with Bcl-2 family proteins
Abstract
Bcl-2 family of proteins plays differential roles in regulation of mitochondria-mediated apoptosis, by either promoting or inhibiting the release of apoptogenic molecules from mitochondria to cytosol. Bcl-2 family proteins modulate the mitochondrial permeability through interaction with adenine nucleotide translocator (ANT), voltage-dependent anion channel (VDAC), ADP/ATP exchange, or oxidative phosphorylation during apoptosis. Although the mitochondrial homeostasis is affected by the relative ratio of pro- and anti-apoptotic Bcl-2 family members, the molecular mechanism underlying the release of mitochondrial intermembrane proteins remains elusive. Here we reported the biochemical evidence that both pro-apoptotic Bax and anti-apoptotic Bcl-X(L) might simultaneously contact the putative loop regions of human VDAC1, and the existence of VDAC1-Bax-Bcl-X(L) tertiary complex in vitro suggested that VDAC1 channel conformation and mitochondrial permeability could be determined by the delicate balance between Bax and Bcl-X(L).
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The N-terminal domain of VDAC1 interacts with several Bcl-2 family proteins that regulate apoptosis and is involved in gating the channel.
“The N-terminal domain of VDAC1 interacts with several Bcl-2 family proteins that regulate apoptosis and is involved in gating the channel [96,97,98,99,100,101].”
From Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease (2020) · cites this paper as [98]
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- Authors
- Shi, Y., Chen, J., Weng, C., Chen, R., Zheng, Y., Chen, Q., & Tang, H.
- Affiliations
- Chinese Academy of Sciences (CN)
- Inner Mongolia Medical University (CN)
- Corresponding author
- Tang, Hong
- Venue
- Biochemical and Biophysical Research Communications
- Publisher
- Elsevier BV
- Published
- 2003-06
- Volume
- 305
- Issue
- 4
- Pages
- 989-996
- ISSN
- 0006-291X (ISSN-L)
- OpenAlex
- W2017490220
- Cited by
- 158
- References
- 54
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 9 · 2023: 13 · 2022: 9 · 2021: 9 · 2020: 7 · 2019: 7 · 2018: 8 · 2017: 10 · 2016: 8 · 2015: 12 · 2014: 7 · 2013: 7 · 2012: 7
- FWCI
- 1.72
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical and Biophysical Research Communications (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Natural Science Foundation of China
- Chinese Academy of Sciences
- 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 › Pathology and Forensic Medicine › Cardiac Ischemia and Reperfusion
- Keywords
- VDAC1, Bcl-2 family proteins, Bax, Bcl-xL, protein-protein interaction, mitochondrial permeability, apoptosis, mitochondrial intermembrane space, voltage-dependent anion channel, channel conformation
- MeSH terms
- Binding Sites, Humans, Protein Binding, Proto-Oncogene Proteins, Mutagenesis, Site-Directed, Protein Structure, Tertiary, Porins, Proto-Oncogene Proteins c-bcl-2, Voltage-Dependent Anion Channels, Voltage-Dependent Anion Channel 1, bcl-X Protein, bcl-2-Associated X Protein
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