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

The DOI matches its Crossref record; 54 of the 54 references it cites were found in a registry or an index.

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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Metadata

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
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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