Voltage-dependent anion channel 1-based peptides interact with Bcl-2 to prevent antiapoptotic activity
Open accessAbstract
The antiapoptotic proteins of the Bcl-2 family are expressed at high levels in many types of cancer. However, the mechanism by which Bcl-2 family proteins regulate apoptosis is not fully understood. Here, we demonstrate the interaction of Bcl-2 with the outer mitochondrial membrane protein, voltage-dependent anion channel 1 (VDAC1). A direct interaction of Bcl-2 with bilayer-reconstituted purified VDAC was demonstrated, with Bcl-2 decreasing channel conductance. Expression of Bcl-2-GFP prevented apoptosis in cells expressing native but not certain VDAC1 mutants. VDAC1 sequences and amino acid residues important for interaction with Bcl-2 were defined through site-directed mutagenesis. Synthetic peptides corresponding to the VDAC1 N-terminal region and selected sequences bound specifically, in a concentration- and time-dependent manner, to immobilized Bcl-2, as revealed by the real-time surface plasmon resonance. Moreover, expression of the VDAC1-based peptides in cells over-expressing Bcl-2 prevented Bcl-2-mediated protection against staurosporine-induced apoptotic cell death. Similarly, a cell-permeable VDAC1-based synthetic peptide was also found to prevent Bcl-2-GFP-mediated protection against apoptosis. These results point to Bcl-2 as promoting tumor cell survival through binding to VDAC1, thereby inhibiting cytochrome c release and apoptotic cell death. Moreover, these findings suggest that interfering with the binding of Bcl-2 to mitochondria by VDAC1-based peptides may serve to potentiate the efficacy of conventional chemotherapeutic agents.
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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 [100]
The Discussion (page unavailable) identifies the VDAC1 N-terminal region as a Bcl-2 interaction site and says evidence suggests it is involved in voltage gating. The paper also discusses VDAC1 interactions with Bax and Bcl-xL, but does not establish that the N-terminal domain itself interacts with several Bcl-2 family proteins. (LLM, conf=0.84)
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- Authors
- Arbel, N., & Shoshan-Barmatz, V.
- Affiliations
- Ben-Gurion University of the Negev (IL)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2010-02
- Volume
- 285
- Issue
- 9
- Pages
- 6053-6062
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC2825399
- OpenAlex
- W1998225262
- Cited by
- 168
- References
- 68
- Citations by year
- 2026: 5 · 2025: 8 · 2024: 8 · 2023: 5 · 2022: 8 · 2021: 11 · 2020: 14 · 2019: 8 · 2018: 18 · 2017: 18 · 2016: 11 · 2015: 9 · 2014: 15 · 2013: 9 · 2012: 11
- FWCI
- 2.82
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Israel Science Foundation
- 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, Bcl-2 family proteins, apoptosis, anti-apoptotic effects, mitochondrial outer membrane, cytochrome c release, staurosporine-induced apoptosis, tumor cell survival, chemosensitization, channel conductance
- MeSH terms
- Animals, Cell Line, Electric Conductivity, Electrophysiology, Humans, Mitochondria, Peptide Fragments, Protein Binding, Sheep, Mutagenesis, Site-Directed, Apoptosis, Proto-Oncogene Proteins c-bcl-2, Surface Plasmon Resonance, Voltage-Dependent Anion Channel 1
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