Cited by 158Cell death mechanisms and regulationMitochondrial Function and PathologyCardiac Ischemia and Reperfusion

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Identification of the protein-protein contact site and interaction mode of human VDAC1 with Bcl-2 family proteins

Shi, Yong, Chen, Jianjun, Weng, Changjiang, Chen, Rui, Zheng, Yanhua, Chen, Quan, Tang, Hong·2003·Biochemical and Biophysical Research Communications

DOI 10.1016/s0006-291x(03)00871-4

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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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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
ORCID: Chen, Jianjun
Weng, Changjiang
Chen, Rui
Zheng, Yanhua
Chen, Quan
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)
DOI: 10.1016/s0006-291x(03)00871-4
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
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
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 › Cardiology and Cardiovascular 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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Identification of the protein-protein contact site and interaction mode of human VDAC1 with Bcl-2 family proteins

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